Final Exam Material Flashcards

(446 cards)

1
Q

What are the fundamental building blocks for proteins?

A

Amino acids

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2
Q

All common amino acids have an asymmetric alpha-carbon.

True or False?

A

False.

Glycine does not.

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3
Q

At pH greater than the isoelectric point (pI) of an amino acids, the net charge is…

A

Negative

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4
Q

At pH lower than the isoelectric point (pI) of an amino acid, the net charge is…

A

Positive

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5
Q

In food systems, what do amino acids provide? [3]

A

Flavour

Colour

Bioactive compounds

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6
Q

What is/are the functional group(s) in proteins and amino acids that can react with reducing sugar in Maillard reaction?

A

Alpha-amino group

Epsilon-amino group

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7
Q

Enzymatic browning shares similarities with Maillard browning and caramelization.

True or False?

A

False.

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8
Q

What does enzymatic browning require? [5]

A

Oxygen

An enzyme

Copper

An aromatic compound as a substrate

A relatively neutral pH

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9
Q

What does decarboxylation of amino acids often lead to?

A

Potentially toxic compounds

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10
Q

Proteins consist only of amino acids.

True or False?

A

False.

They may have additional groups, e.g., carbs, lipids, etc.

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11
Q

What does the primary structure of a protein refer to?

A

The sequence of amino acids.

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12
Q

The alpha helix of proteins is stabilized by hydrophobic bonds.

True or False?

A

False.

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13
Q

The alpha helix of proteins is often the most stable secondary protein structure.

True or False?

A

True.

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14
Q

The beta sheet of secondary protein structure is comprised of beta strands.

True or False?

A

True.

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15
Q

The tertiary structure of a protein is stabilized by…

A

Numerous bonds/forces

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16
Q

Where does a hydrogen bond occur?

A

Between a hydrogen and an electronegative atom

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17
Q

How may disulfide bonds be broken?

A

By a reducing agent

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18
Q

Define: protein denaturation

A

Any change in the secondary, tertiary and/or quaternary structure without cleavage of the protein backbone.

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19
Q

Name 4 functional properties of proteins (not an exhaustive list)

A

Water solubility

Gelation

Emulsification

Viscosity

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20
Q

When is the water binding capacity of most proteins at its lowest?

A

At its isoelectric point

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21
Q

When a protein denatures, what happens to its emulsifying properties?

A

They increase

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22
Q

What happens to the emulsifying properties of a protein when its solubility increases (e.g., by pH changes, salt addition, etc.)?

A

They increase

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23
Q

Why are proteins good foaming agents?

A

They surround a gas phase

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24
Q

Presence of salts at low concentrations increases which properties of most proteins? [4]

A

Solubility

Water binding capacity

Water holding capacity

Emulsifying ability

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25
When does a coagulum type gel result?
From hydrophobic bonds and possibly disulfide linkages
26
At extreme pH, protein gels are the strongest due to covalent linkages. True or false?
False. At extreme pH, protein gels are weakest due to charge properties.
27
What does curd formation in milk result from?
Enzyme action causing an increase in hydrophobicity of the micelle
28
What are amino acids? [3]
* Alpha-amino acids are the basic structural units of proteins * Consist of an alpha-carbon atom covalently attached to a hydrogen, an amino group, a carboxyl group, and a side chain R group. (Contains C, H, O, & N, [S, P]) * Amino acids differ only in the chemical nature of the side chain of the R group
29
Describe the structure of an amino acid.
The alpha carbon is an asymmetric carbon atom in all amino acids (except for glycine), thus amino acids exist in two optically active forms: L- and D- isomers.
30
L-isomer amino acids are sweet and D-isomers are bitter. True or False?
False.
31
Describe the solubility of amino acids. [2]
* Differences in solubility of properties of amino acids is due to the type of side chain. * Dependent on the dissociation properties of the amino acid, known as dissociation constant (pKa)
32
What are the essential amino acids?
Essential amino acids cannot be synthesized *de novo* by the organism, and must be supplied in the diet. **PVT TIM HLL** Phenylalanine Valine Tryptophan Threonine Isoleucine Methionine Histidine Arginine Leucine Lysine
33
What are limiting amino acids? [3]
* Quality of proteins depends on the richness of essential amino acids (limiting amino acids) and the digestibility of the protein. * A limiting amino acid is the essential amino acid found in the smallest quantity in the food (e.g., gelatin lacks 4 eAA) * Limiting amino acids affect the net protein utilization or biological value
34
Different amino acids provide different physicochemical properties to peptide chains or protein molecules. Describe how valine, isoleucine, and leucine are similar?
These three amino acids have nonpolar side chains that are branched and thus restrict the internal flexibility and give rise to surface hydrophobicity.
35
Different amino acids provide different physicochemical properties to peptide chains or protein molecules. Describe how serine and threonine are similar.
Polar side chains form hydrogen bonds. Serine and threonine have hydroxyl groups that form hydrogen bonds.
36
Different amino acids provide different physicochemical properties to peptide chains or protein molecules. Describe the uniqueness of cysteine.
Cysteine has an important role in forming sulfydryl (S-S) bridges between different parts of the peptide chain.
37
Describe the role of glutamate in foods. [2]
* L-glutamate suppresses certain ‘undesirable’ flavours, such as: * Sharpness of onion flavour * Rawness in many veggies * Earthiness of potatoes * Glutamate activity to modulate taste in foods is noticeable between pH 3.5 to 7.2, being more intense in lower pH.
38
Describe sweetness perception of amino acids. [6]
* D-amino acids generally evoke a sweet taste perception while L-amino acids are tasteless or bitter. * Short side-chain of L-amino acids can also elicit a sweet taste * As the side chain length of L-amino acids increases, the sweetness will change to bitter * If the hydrophobicity increases on the L-amino acid, the sweetness will be lost and replaced either with bitter or no taste. * Preference for D-amino acids tend to increase with molecular weight and hydrophobicity. * The correlation between the hedonic score and D-amino acid molecular weight or bulk of the side chain reflects that the lower threshold score, the less required from the sample to elicit a positive preference.
39
What reaction has the greatest impact on protein sensory and nutritional properties?
Maillard reaction, which occurs in both food and biological systems. Amino component → proteins and amino acids Carbonyl component → reducing sugars, ascorbic acid (vitamin C) and carbonyl compounds
40
Describe Strecker degradation. [4]
* The 3rd pathway of the Maillard reaction; carbonyl-amine reaction * The oxidation of amino acids by an alpha-dicarbonyl or other conjugated dicarbonyl compound that is produced on the breakdown of Amadori compounds * Amino acids are degraded to aldehydes, pyrazines, sugar fragments, ammonia, and carbon dioxide. * Strecker degradation of each amino acid produces a specific volatile compound and provide unique aromas and flavours
41
What are amino acids degraded to during Strecker degradation, the 3rd pathway of the Maillard reaction? [5]
Aldehydes, pyrazines, sugar fragments, ammonia, and carbon dioxide.
42
Describe tyrosine oxidation.
* The presence of oxygen and the enzyme tyrosinase are essential for the oxidation of tyrosine to dihydroxyphenylalanine (DOPA) * Copper is an essential co-factor for tyrosinase enzymatic activity * Optimal pH ranges from 6.7 - 7.2 * Sequestering copper agents (e.g., organic acids) and decreasing pH result in the inhibition of tyrosinase * The reaction is also reduced by: * Reduction of oxygen concentration (i.e., vacuum packaging) * Use of reducing agents (e.g., ascorbic acid, sulfites)
43
What does tyrosine oxidation require?
Tyrosinase (and a copper cofactor catalyst) pH 6.7 - 7.2
44
What reduces tyrosinase activity?
Sequestering copper agents (e.g., organic acids) Reducing of oxygen concentration (e.g., vacuum packaging) Use of reducing agents (e.g., ascorbic acid, sulfites)
45
How are biogenic amines formed? [3] | (e.g., vasoactive amines)
* Amino acid decarboxylation reactions result in their formation * Tyrosine to tryamine * Histidine to histamine * Phenylalanine to phenylethylamine * Arginine to putrescine * Bioactive amines are the result of the action of the bacterial enzyme: L-amino acid decarboxylase
46
What is tyramine?
* Formed by decarboxylation reaction catalyzed by bacterial L-amino acid decarboxylase. * Naturally present in small amounts in bananas, pineapples, and produced by *streptococci* action in cheddar cheese * Poisoning can occur as low as 40mg * Causes hypertension and intense headaches
47
What is histamine and how is it formed? [6]
* Decarboxylation reactions * Formed from the enzymatic action of gram-negative bacteria mainly found in fish * Poisoning symptoms include headache, nausea, hypertension, and vomiting * Histamine production can also be synthesized by the normal flora of the colon. * Intake of foods rich in histadine may favour endogenous production of histamine * Histidine decarboxylase is also present in tissue mast cells and blood cell basophils, thus typical signs of inflammation can be due to the release of this enzyme.
48
Typical signs of inflammation may be due to…
Release of histidine decarboxylase, present in mast cells and blood cell basophils.
49
What is putrescine and how is it formed?
Decarboxylation reaction
50
What is tryptamine and how is it formed?
Decarboxylation reactions
51
Describe the cause of amino oxidation product formation, which amino acids are involved, and the consequences. [7]
* Protein in different food matrices like beef patties, chicken meat, raw pork, and different types of fish can be oxidized during frozen storage * The usage of sodium nitrite, in cured meat, is another cause of protein oxidation. * Specific amino acids are involved * Lysine (alpha-aminoadipic acid) * Tyrosine (kynurenine) * Tryptophan (kynurenic acid) * Consequences → protein functionality and human health
52
Which alpha-amino acids contain ionizable groups? [6]
Proline Tryptophan Tyrosine Cysteine Arginine Histidine
53
What are nitrites used for?
Preservation against *C. botulinum*
54
What is nitrite reduced to? What does it react with? What does it form?
Nitrous anhydride, which reacts with amines containing ionizable groups, forming *nitrosamines* (risk of cancer) Nitrosamides are derivatives of substituted amines
55
Under what conditions are nitrosamines produced?
Conditions of low pH (stomach environment) and at high temperatures (frying, roasting)
56
When are nitrosamines carcinogenic?
When metabolically activated by the hosts' oxidative enzymes
57
What are proteins? [3] Next to water, protein is the most plentiful substance in the body!
* Organic compounds formed by 100-500 amino acids linked together * Necessary in the diet, since not all amino acids can be synthesized * Built from a central carbon bonded to four *different* groups * Hydrogen * Amino group * Carboxyl group * Side chain
58
Simple proteins yield amino acids upon hydrolysis. Name 4 types of simple proteins and describe their solubility.
* **Albumins** → soluble in water * **Globulins** → soluble in neutral salt solutions * **Glutelins** → soluble in dilute acid or alkali * **Prolamins** → soluble in 70% alcohol
59
What are conjugated proteins?
Proteins that contain amino acids combined with a non-protein constituent.
60
What are phosphoproteins?
A conjugated protein Phosphate groups linked to hydroxyl groups of serine or threonine E.g., casein in milk and phosphoprotein in yolk
61
What are lipoproteins
Conjugated proteins Combination of lipids and protein with excellent emulsifying properties
62
What are nucleoproteins?
Conjugated proteins Combination of nucleic acid with protein Found in cell nuclei
63
What are glycoproteins?
Conjugated proteins With carbohydrate (8-20%) Has strong allergenic properties E.g., ovomucin in egg white
64
What are chromoproteins?
Conjugated proteins Have prosthetic groups E.g., hemoglobin, chlorophyll, myoglobin, flavoproteins
65
What are derived proteins?
Derived proteins are obtained by chemical or enzymatic methods. They are soluble in water and not coagulated by heat.
66
What are primary-protein derivatives?
Limited hydrolyzed proteins - coagulated proteins E.g., rennet coagulated casein
67
What are secondary protein derivatives?
Peptones and peptides: a combination of two or more amino acids Examples are the breakdown products formed during processing of milk products: the peptides formed during the ripening of cheese
68
What is the primary structure of a protein?
Primary structural properties of proteins → sequence of amino acids Associated with the properties of individual amino acids comprising the protein Amino acids are linked by covalent bonds through amide bonds, also known as peptide bonds.
69
What is the secondary structure of a protein?
* Refers to the periodic spatial arrangement of amino acid residues at certain segments of the polypeptide chain * The regularly repeating local structures are stabilized by hydrogen bonding; notable examples are the alpha helix, beta sheet, beta turns, and random coil * Two forms of periodic secondary structures are found in proteins: helical and sheet structures. * Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.
70
Describe the alpha-helix secondary structure. [5]
* From the helical structures the major form in proteins is the alpha-helix, which is the most stable * Each backbone N-H group is hydrogen bonded to the C=O group of the fourth preceding residue * Can exist in either right or left-handed orientation → the right-handed helix is more stable * The helix makes a complete turn every 3.6 amino acids. * In the alpha-helix, the backbone atoms form a coil while the carbonyl groups form hydrogen bonds with the amide groups
71
The left-handed alpha-helix is the most stable. True or False?
False. The right-handed alpha-helix is more stable.
72
How many amino acids in a complete turn of an alpha-helix?
3.6
73
Describe the beta-sheet secondary structure of proteins. [8]
* The C=O and N-H groups are oriented perpendicular to the direction of the chain * Hydrogen bonding is possible between segments but not within a segment * Comprised of individual beta-strands usually 5-15 a.a. long * Two beta-strands of the same molecule interact by hydrogen bonds, forming a beta-pleated sheet * Beta-strands often have a hydrophilic and hydrophobic side * Beta-sheet is generally more stable than the alpha-helix * Fibrous in nature and insoluble in aqueous solvents * E.g., soy globulin, beta-lactoglobulin
74
Which is more stable, alpha-helix or beta-sheet?
Beta-sheet
75
Beta-sheet structure is generally fibrous in nature and soluble in aqueous solvents. True or False?
False. They are INSOLUBLE in aqueous solvents (they are fibrous in nature).
76
Beta-strands in beta-pleated sheets run antiparallel. True or False?
May be parallel or antiparallel. Anti-parallel beta-sheets are stronger than parallel due to the hydrogen bonds lying on the same plane.
77
What is the tertiary structure of proteins?
* Refers to the spatial arrangement attained when a linear protein chain with defined (alpha-helix or beta-sheets) or non-defined (random coil) secondary structure segments folds further into a compact 3D form. * Amino acid linkages fold over into compact structures stabilized by hydrogen bonds, disulphide bridges, and van der Waals forces.
78
What does quaternary structure of a protein refer to?
The spatial arrangement of a protein when it contains more than one polypeptide Formation of oligomeric structures is the result of specific protein-protein interactions
79
What interactions determine the secondary and tertiary structure of proteins? [5]
Hydrogen bonds van der Waals forces Hydrophobic interactions Disulfide linkages Ionic interactions
80
Describe the following forces governing protein structure: Covalent Ionic Hydrogen Hydrophobic Electrostatic repulsion van der Waals repulsion
* **Covalent** → atoms bound by a common electron pair e.g., peptide bonds, disulfide bonds * **Ionic** → attraction between opposite forces e.g., solvent interaction, salt working * **Hydrogen →** hydrogen shared between two electronegative atoms; stabilizing/bridging * **Hydrophobic** → apolarity; strand thickening, strengthening, stabilizing * **Electrostatic** **repulsion** → coulombic repulsion between particles with like-charges e.g., polar groups of side chains * **van der Waals repulsion** → repulsion of apolar groups that are close; steric hindrance between side chain groups
81
What is a hydrogen bond?
Interaction of a hydrogen atom that is covalently bonded to an electronegative atom (N, O, S) with another electronegative atom.
82
Describe how proteins fold into unique tertiary structures and what its stability depends on. [3]
* Protein stability depends on maintenance of an apolar environment * Hydrophobic interactions are the major forces to drive protein folding and stability * Hydrophobic interaction between nonpolar side chains of amino acid residues is the major reason by which proteins fold into unique tertiary structures.
83
What is the main reason by which proteins fold into unique tertiary structures?
Hydrophobic interactions
84
Describe disulfide bonds.
* Disulfide bonds occur between two cysteine (Cys) resides by oxidation of the sulfhydryl groups by molecular oxygen. * Once formed, disulfide bonds help stabilize the folded structure of the protein.
85
What are causes of protein denaturation? [5]
* Acids * Strong salt solutions * Heat * Alkaline conditions * Radiation
86
Protein denaturation is irreversible. True or False?
False. Protein denaturation is usually reversible (in the absence of aggregation) when the denaturant is removed (except egg white).
87
Many biologically active proteins lose their activity upon denaturation. Denaturation may result in: [6]
* Loss of solubility * Increase intrinsic viscosity * Altered water holding capacity * Increased digestibility * Increase susceptibility to protease attack * Improves foaming and emulsifying properties
88
Many biologically active proteins lose their activity upon denaturation. Denaturation may result in: [6]
* Loss of solubility * Increase intrinsic viscosity * Altered water holding capacity * Increased digestibility * Increase susceptibility to protease attack * Improves foaming and emulsifying properties
89
Describe how a protein's primary, secondary, tertiary, and quaternary structure change with denaturation.
* **Primary** structure is not disrupted. * **Secondary** structure → proteins lose all regular repeating patterns like alpha helices and beta pleated sheets and adopt a random coil configuration. * **Tertiary** structure → covalent interactions (like disulfide bonds), non covalent interactions between polar side chains and surrounding solvent, and v.dw. interactions between non polar amino acid side chains are all disrupted * **Quaternary** → protein sub-units are dissociated and/or the spatial arrangement of protein subunits is disrupted
90
Functionality of food proteins is defined as “those physical and chemical properties which affect the behaviour of proteins in food systems during processing, storage, preparation, and consumption”. (Kinsella, 1976) List the functional roles of proteins in food systems. [10]
1. Solubility 2. Viscosity 3. Water binding 4. Gelation 5. Cohesion-adhesion 6. Elasticity 7. Emulsification 8. Foaming 9. Fat binding 10. Flavour binding
91
What groups in proteins will water bind to? [5]
* Charged groups: ion-dipole interaction * Backbone peptide groups * Amide groups of Asn and Gln * Hydroxyl groups of Ser, Thr, and Tyr residues * Non-polar residues, dipole-induce dipole interaction and hydrophobic interaction
92
Define water binding capacity.
Grams of water per gram of protein when a dry protein is equilibrated with water vapour at 90-95% relative humidity. Also known as hydration capacity.
93
What three factors influence water binding capacity?
pH and isoelectric point Presence of salts Temperature
94
How does pH and isoelectric point affect water binding capacity?
* At the isoelectric point, proteins exhibit the least hydration, but greatest protein-protein interaction * Water binding capacity increases above and below the isoelectric pH * The greatest is usually at pH 9-10 * Exposure of groups
95
Describe how presence of salts affects water binding capacity of proteins.
* At low concentrations (\<0.2M), salts increase water binding capacity. Hydrated salt ions bind weakly to charged groups of proteins - “**salting in**” * At high salt concentration, water is bound to salt ions, resulting in dehydration of the protein - “**salting out**”
96
Describe how temperature affects the water binding capacity of proteins.
* As temperature is raised, water binding capacity generally decreases because of decrease in hydrogen bonding and decrease in hydration of ionic groups * If temperature leads to aggregation, water binding capacity decreases due to increase in protein-protein interactions
97
Define water holding capacity.
Refers to the ability of the protein to imbibe water and retain it against gravitational force within a protein matrix. Refers to the (1) sum of bound water, (2) hydrodynamic water, and (3) the physically entrapped water.
98
The contribution of physically entrapped water is lesser than those of the bound and hydrodynamic water. True or False?
False. Its contribution is larger than those of the bound and hydrodynamic water.
99
What is the ability of protein to entrap water associated with?
Juiciness and tenderness of meat products Desirable textural properties of bakery and other gel-type food products.
100
What is an emulsification?
A mixture of two immiscible substances, stabilized by emulsifiers.
101
Describe the emulsification properties of proteins.
* Proteins in native form act as emulsifiers by having hydrophobic amino acids hidden, or protected from the water phase, by hydrophilic amino acids. * On denaturation, the protein unfolds and hydrophobic amino acids align with non-polar or oil phase and the hydrophilic amino acids align with polar or aqueous phase.
102
Describe how proteins are emulsifiers for oil in water (o/w) emulsions.
Because they are edible, surface active, and provide superior resistance to coalescence They provide amphiphilic domains With adsorption, native conformation is changed: side chains of hydrophobic amino acids → to surface of oil droplet; hydrophilic amino acid side chains remain in aqueous solution Result = water-oil interface
103
Describe how proteins are the emulsifiers in water in oil (w/o) emulsions.
They cannot be used for (w/o) emulsions because of insolubility in oil. Reduces interfacial tension.
104
Describe five factors that affect protein emulsification.
1. **Solubility of protein** → optimal at 25-80% solubility 2. **pH** → proteins with high solubility at their isoelectric point have maximal emulsifying capacity. 3. **Salt** → may increase protein solubility thereby increasing emulsification 4. **Temperature** → small increase in temperature will influence the rate of diffusion and the rate of adsorption and protein unfolding thus increasing emulsification 5. **Denaturation** → with partial denaturation, proteins start to unfold so that free sulfhydryl groups and disulphide bonds form interactions at the oil/water interface = increase flexibility and surface hydrophobicity = increase emulsification
105
Describe protein foaming.
* A foam consists of an aqueous continuous phase and a gaseous (air) phase * The foaming property of a protein refers to its ability to form a thin tenacious film at gas-liquid interfaces so that large quantities of gas bubbles can be incorporated and stabilized * Protein-stabilized foams are formed by bubbling, whipping, or shaking a protein solution
106
Describe flavour binding properties of proteins. [4]
* Proteins themselves are odorless. * Flavours come mainly from aldehydes, ketones, and alcohols * Noncovalent interactions are normally the mechanism of flavour binding to proteins; covalent bonding may also happen * Only the noncovalently bound fraction can contribute to aroma and taste of the protein food
107
Describe 5 factors that affect flavour binding properties of proteins.
1. **Protein denaturation** → thermally denatured proteins exhibit increased ability to bind flavours; ability to bind flavours is lower in denatured than in native proteins 2. **Salts** → ‘salting in’ destabilize hydrophobic interactions, thus decreasing flavour binding; ‘salting out’ increases flavour binding 3. **pH** → flavour binding is enhanced at alkaline pH 4. **Disulfide bonds** → breakage of disulfide bonds causes unfolding of proteins thus increasing flavour binding 5. **Proteolysis** → hydrolysis of protein causes disruption and decreases hydrophobic regions and thus decreases flavour binding; proteolysis usually produces peptides of bitter taste
108
What is gelation?
Protein gelation refers to the transformation of a protein from a solid state to a gel-like state. Two types → coagulum and translucent
109
Describe coagulum gel (opaque gel).
**Irreversible gel** Original protein have large amounts of non-polar residues that undergo hydrophobic aggregation, or insoluble aggregates that **randomly associate**
110
Describe translucent gel.
* Main linkages are H-bonds and electrostatic forces * Formed by proteins with relatively small amounts of insoluble residues and high amounts of polar amino acid residues * **Reversible** soluble complex after denaturation * **Ordered aggregation**
111
What is a gel network mainly formed by?
Hydrogen bonding and hydrophobic and electrostatic interactions
112
Gels are highly hydrated systems, up to 98% water. True or False?
True.
113
What type of gel is less prone to syneresis and why?
Translucent gels hold more water and are less prone to syneresis than coagulum-type gels, due to hydrogen bonding interactions.
114
Describe how the type of interaction affects protein gelation.
* Gels formed by noncovalent interactions, mainly hydrogen bonds, are thermally reversible * Gels formed by hydrophobic interactions are irreversible (e.g., egg white gel) * Proteins can undergo polymerization via sulfhydryl-disulfide interactions → usually thermally irreversible (e.g., whey gels)
115
Describe how protein concentration affects gelation.
Minimum point concentration, least concentration end point (LCE) is required Soy protein = 8% Egg albumin = 3% Gelatin = 0.6%
116
Describe how humectants (sugars or salts) affect protein gelation.
Humectants bind to free water causing high protein-protein interaction and low protein-water interaction This results in strong gels formation with greater heat stability.
117
Describe how pH affects protein gelation.
* At or near pI, proteins usually form a coagulum-type gel. * Acid conditions increase the amount of free water, thus decreasing the negative charge and increasing aggregate formation * Extreme pH → weak gels are formed because of strong electrostatic repulsion * Optimum pH = 7-8 for most proteins
118
Describe how proteolysis affects protein gelation.
* Limited proteolysis facilitates gel formation * Addition of chymosin (rennin) to casein in milk results in formation of coagulum-type gel
119
Describe how cross-linking affects protein gelation.
* Enzymatic cross-linking at room temperature can result in gelation * Transglutaminase is used to form highly elastic and irreversible gels, even at low protein concentration
120
List 6 factors affecting protein gelation.
1. Type of interaction 2. Protein concentration 3. Humectants (sugar or salt) 4. pH 5. Proteolysis 6. Cross-linking
121
How much protein is in milk?
Bovine milk contains 30-36 g/L (%) of total protein Milk proteins: casein (80%) and whey (20%)
122
Describe casein.
* Mainly alpha, beta, and kappa caseins * Calcium sensitive alpha and beta (addition of calcium precipitates protein); kappa caseins are calcium insensitive (addition of protein will not affect protein, it remains soluble) * Amphipathic * Self-associate in solution to form micelles
123
Describe how the rennin enzyme affects casein micelles.
* It cleaves k-casein at Phe105 - Met106 into para-k-casein and a glycopeptide * para-k-casein micelles form small aggregates, which then assemble into a gel
124
Compare the hydrophobicity, and calcium binding capacity of alpha beta and kappa casein.
**(1) Hydrophobicity** * αs2- **(2) Calcium binding capacity** * The higher degree of phosphorylation, the higher binding capacity to calcium. * αs2- \> αs1- \> β- \> κ-
125
Describe the interactions of casein micelles.
Micelles are kept together by electrostatic interactions: * Calcium or calcium phosphate bridges with phosphoserine and glutamic residues * Hydrogen bonds and minimal hydrophobic bonding
126
Lipids are formed from structural units with a pronounced hydrophobicity. True or False?
True
127
Lipids are generally insoluble in water but some are amphipathic molecules. True or False?
True.
128
The nutritive/physiological importance of lipids is based on their role as energy molecules (e.g., 4 kcal/gm) and a source of essential fatty acids and vitamins. True or False?
False. 9 kcal/gm
129
A refined lipid is available to consumers as an edible oil or fat. True or False?
True.
130
The acyl residue has no influence on the hydrophobicity and reactivity of acyl lipids. True or False?
False.
131
Fatty acids are not saponifiable. True or False?
False
132
Phospholipids are saponifiable. True or False?
True.
133
Waxes are saponifiable. True or False?
False.
134
Acyl lipid hydrolysis releases aliphatic carboxylic acids which differ in chemical structure. True or False?
True.
135
In general, it is true from the percentage data of fatty acid distribution that the unsaturated fatty acids predominate. True or False?
True.
136
C18:2 Δ9,12 refers to linoleic acid. True or False?
True.
137
Milk and coconut fats mainly consist of short chain, low molecular weight fatty acids ( True or False?
True.
138
Stearic acid is a long chain monosaturated fatty acid. True or False?
False.
139
Eicosanoic acid is a HUFA found in lard. True or False?
False
140
In the omega (ω) numbering system of unsaturated fatty acids, position of the first double bond (*n*) starts by counting from the methyl end of the hydrocarbon chain. True or False?
True
141
*cis*-Oleic acid falls in the omega-9 family, where *trans*-Elaidic acid is an omega-6 fatty acid. True or False?
False.
142
Melting properties of fats are determined by the arrangement of the acyl residues in the crystal. True or False?
True.
143
The solubility of fatty acids increases with an increase in the number of *cis*-double bonds. True or False?
True.
144
Lipases derived from the pancreas hydrolyze triacylglycerols at acyl residue positions 1 and 3. True or False?
True.
145
Acyl lipid constituents, such as oleic, linoleic, and linolenic acids, have one or more allyl groups within the fatty acid molecule which makes them readily oxidized to hydroperoxides. True or False?
True
146
Lipid peroxidation provides numerous volatile and nonvolatile compounds, some being pleasant while others objectionable. True or False?
True.
147
What does the length of induction period and the rate of oxidation depend on? [3]
* Fatty acid composition of the lipid * The number of allyl groups present * The presence of antioxidants.
148
Briefly describe the oxidation of lipids. [4]
* Radical-induced chain reaction * Divided into initiation, propagation, and termination phases * Involves abstracting the H-atoms from activated methylene groups on unsaturated fatty acids * Culminating into formation of non-hydroperoxide molecules
149
Which step of lipid oxidation are heavy metals involved in?
The initiation reactions
150
The peroxyl radical is slow reacting and therefore it selectively abstracts the most weakly bound H-atom from a fat molecule. True or False?
True.
151
What does initiation of lipid oxidation require? [3]
Photosensitizers Lipoxygenases Transition metal ions
152
In the ground state oxygen is a triplet. True or False?
True.
153
Oxygen goes from triplet state to singlet oxygen state by uptake of energy. True or False?
True.
154
With oleic acid, the singlet state of oxygen attacks the 9-10 double bond generating 2 mono-hydroperoxides. True or False?
True.
155
The primary products of autooxidation, mono-hydroperoxides, are odorless and tasteless. True or False?
True.
156
Volatile carbonyl compounds are the main aroma carriers in lipid peroxidation. True or False?
True.
157
Volatile carbonyls are formed by beta-scission of the mono-hydroperoxides. True or False?
True
158
Products of beta-scission include short lived alkoxyl radicals. True or False?
True.
159
Beta-scission can be catalyzed by heavy metal ions or heme compounds. True or False?
True.
160
Describe steroid structure. [3]
Includes 4 condensed rings with the first 3 being in the chair configuration and the last one being planar. Rings B and C, and C and D are fused by *trans*-configuration, rings A and B are fused in *trans-* or *cis-* configuration. A characteristic of steroids is the presence of alcoholic OH-group in position C3.
161
Cholesterol is the main steroid in mammals and occurs in lipids in only free form. True or False?
False.
162
Cholesterol in egg yolk is less than that in butter, when compared in the same weight of food (e.g., mg cholesterol per 100 g egg yolk or butter). True or False?
False
163
Autooxidation of cholesterol can be accelerated by fatty acid oxidation products. True or False?
True.
164
Cholesterol oxidation can be measured by TBARS assay. True or False?
False.
165
TBARS assay aims to measure the primary product of lipid oxidation. True or False?
False.
166
TBARS assay aims to measure the secondary product of lipid oxidation. True or False?
True.
167
TBARS assay requires colorimetric or fluorometric measurement. True or False?
True.
168
TBARS assay is useful for comparison of samples with significantly different compositions. True or False?
False.
169
What does the TBA assay for quantitating lipid oxidation in pure oil require? [3]
* Butylated hydroxytoluene (BHT) * A blank without lipid sample * Construction of a standard curve
170
Quantification of peroxide value (PV) correlates well with off-flavours and off-aromas in oxidized lipid samples. True or False?
False.
171
Peroxide value of herring oil during 50 degrees C storage was lower than that during 20 degrees C storage because higher temperature suppresses lipid oxidation. True or False?
False.
172
Quality of lipid food is not affected until secondary volatile aldehydes and ketones are formed in lipid oxidation. True or False?
True
173
Sensory evaluation is a direct method for evaluating off-flavours and off-aromas associated with lipid oxidation. True or False?
True.
174
Lipids are fat-soluble (i.e., lipophilic molecules), and only soluble in organic solvents. True or False?
True. However, some lipids are surface active since some are amphipathic molecules. (e.g., phospholipids)
175
Oils are liquid while fats are solid at room temperature. True or False?
True.
176
What are the main biological functions of lipids? [3]
Energy storage (9 kcal/g) Structural component of cell membranes Signalling molecules
177
What are some functions of lipids in foods?
Influence flavour and texture Many fat soluble vitamins require lipids for bioavailability; low fat diets will reduce the absorption of lipid soluble vitamins (A, D, K, E) Can be used as a cooking medium
178
What are the fat soluble vitamins?
A D E K
179
What are the non saponifiable lipids? [3]
**Simple lipids** Free fatty acids Isoprenoid lipids (i.e., steroids, carotenoids, monoterpenes) Tocopherols
180
What are saponifiable lipids? [6]
**Acyl lipids** Mono-, di-, triacyl- glycerols Phospholipids Glycolipids Diol lipids Waxes Sterol esters
181
What are neutral lipids? [6]
Fatty acids (\> 12-C) Mono-, di-, triacyl- glycerols Sterols, sterol esters Carotenoids Waxes Tocopherols
182
What are polar (amphiphilic) lipids? [4]
Glycerophospholipids Glyceroglycolipids Sphingophospholipids Sphingoglycolipids
183
What are the most abundant class of food lipids?
Acylglycerols [= Esters (glycerol + fatty acids)] The acyl residues influence the hydrophobicity and reactivity of the acyl lipids.
184
Milk fats are unique in short chain and medium chain fatty acids (C4-C12). True or False?
True
185
Lauric acids (e.g., coconut) are unique in high content of lauric (50%) and long chain triglycerols (\>C18). True or False?
False. They are unique in high content of lauric acid (50%) and medium chain triglycerols (C6-C10)
186
Vegetable butters (e.g., cocoa butter) have a wide melting range. True or False?
False. High saturated:unsaturated ratio Narrow melting range.
187
Oleic-linoleic acids are unsaturated. True or False?
True. Most abundant, all vegetable origin.
188
Linolenic acids are n-6 vegetable oils (soybean, rapeseed, hemp, etc.) True or False?
False. They are n-3
189
Off-flavours are easily generated from n-3 vegetable oils (linolenic acids) True or False?
True
190
Briefly describe animal fats (e.g., lard and tallow). [2]
C 16 - C 18 Cholesterol present
191
Marine oils (long-chain n-3 HUFA) are more resistant to oxidation compared to animal fats. True or False?
False. They are less resistant to oxidation and rancidity compared to animal fats. They have multiple unsaturated fatty acids.
192
How are fatty acids classified according to saturation?
Saturates Monounsaturates (omega-9) Polyunsaturates (omega-6, omega-3)
193
How is melting point affected by the length of the saturated fatty acid?
Generally as chain length increases melting point increases as well.
194
C12:0 Lauric acid Saturated fatty acid
195
C16:0 Palmitic acid Saturated fatty acid
196
C14:0 Myristic acid Saturated fatty acid
197
C18:0 Stearic acid Saturated fatty acid
198
C18:1 n9 Oleic acid Unsaturated fatty acid
199
C18:3 n3 linolenic acid Unsaturated fatty acid
200
C18:2 n6 linoleic acid Unsaturated essential fatty acid
201
C20:4 n6 Arachidonic acid Long-chain unsaturated fatty acid
202
C20:5 n3 Eicosapentaenoic acid Long-chain unsaturated fatty acid Found in fish oils
203
C22:5 n3 Docosapentaenoic acid Long-chain unsaturated fatty acid Found in fish oils
204
Describe the omega-9 elongation and desaturation pathway.
Oleic acid * Desaturation* * Elongation* * Desaturation* Palmitoleic or Eicosatrienoic acid
205
Describe the omega 6 elongation and desaturation pathway.
Linoleic acid (EFA) * Desaturation* * Elongation* * Desaturation* Arachidonic acid
206
Describe the omega-3 elongation and desaturation pathway.
Alpha-linolenic acid (EFA) * Desaturation* * Elongation* * Desaturation* * Elongation* * Desaturation* Docosahexaenoic acid
207
What is *cis*-conformation?
* Double bonds of unsaturated fatty acids an be either in the *cis-* or *trans-* conformation * A *cis* configuration means that adjacent carbon atoms are on the same side of the double bond * The *cis* isomer causes the chain to bend and restricts the conformational freedom of the fatty acid.
208
What is *trans*-conformation?
* A *trans* configuration means that the next two carbons are bound to opposite sides of the double bond * *Trans* configuration does not cause the chain to bend much, and their shape is similar to straight saturated fatty acids
209
What are triacylglycerols?
The main constituents of vegetable oils and animal fats. A.K.A. triglycerides Fatty acids esterified to glycerol
210
What are phospholipids?
These molecules are made from glycerol, two fatty acids, and (in place of the 3rd fatty acid) a phosphate group, with another molecule attached to the other end. The hydrocarbon tails of the fatty acids are hydrophobic, but the phosphate group end of the molecule is hydrophilic because of the oxygen constituents with all pairs of unshared electrons (= phospholipids are soluble in both water and oil)
211
What is polymorphism?
* The property of fats to exist in different crystalline phases/forms while having the same chemical composition. * The crystalline forms have a specific melting point, solubility, density, and heat of fusion. * Upon melting polymorphic forms yield identical liquid phases. * Polymorphism plays a significant role in the sensory attributes of the lipids (e.g., texture, mouthfeel, and gloss)
212
Describe the process of triacylglyceride crystallization.
* Triacylglycerides aggregate together to form highly ordered structures, called *nuclei.* * Nuclei serves as points of crystal growth (e.g., crystallization) * Nuclei are precursors of crystalline structures * Each of the triacylglyceride polymorphs possesses specific crystal characteristics * Melting properties are determined by the arrangement of the acyl residues in the crystal lattice.
213
What are the three primary polymorphic forms of triacylglyceride polymorphs?
There are three primary polymorphic forms: α, β, and β’ α → unstable due to high degree of disorder; random order chain axis; do not align efficiently or pack tightly; usually small and numerous β → packed to a much greater extent compared to alpha with more aligned structures; allows formation of larger crystals; greater stability and can achieve longer lengths; more likely to accumulate in fats β’ → parallel rows with the same orientation opposite to orientation of rows above and below; larger than α; smaller than β Conversion of β to β' is done in the production of margarine for example which allows a softer/spreadable fat.
214
How is the melting point of fats influenced by the degree of crystallization?
**Beta** → highest MP **Beta-prime** → intermediate MP **Alpha** → lowest melting point Species of fatty acids present (e.g., chain length, saturated/unsaturated, cis/trans) affects which type of crystal will form
215
Discuss the cooling parameters for formation of triglyceride polymorphs.
alpha → rapid cooling beta-prime → slow cooling beta → very slow cooling
216
What type of polymorph is desired in the manufacturing of margarine?
Beta-prime crystals Allows low-temperature spreadability and storage and high-plasticity
217
What are major factors involved in lipid oxidation of meat systems?
Membrane phospholipids (substrate) Pro-oxidants (hemoglobin & myoglobin) Presence of antioxidants
218
What does autooxidation involve?
The oxidative deterioration of lipids with molecular oxygen via a self-catalytic mechanism. Singlet oxygen is the excited state of oxygen which is usually generated by a photosensitizer pigment, and is less stable than triplet oxygen. Singlet oxygen has the same quantum state of food nutrients, therefore it can react more readily (1500x) than triplet oxygen.
219
Draw a schematic mechanism of the 3 phases of lipid oxidation resulting in lipid rancidity.
Initiation Propagation Termination
220
Describe the initiation phase of lipid oxidation.
* Characterized by the abstraction of a hydrogen atom from a methylene carbon that is located in between two double bonds of the unsaturated fatty acid. * Has a fairly high energy of oxidation, which is why pro-oxidants are required to initiate the reaction * Yields a carbon-centered radical
221
How does the degree of unsaturation affect the rate of lipid oxidation?
Concentration of the unsaturated fatty acid is in the rate law Induction period is affected by the type of unsaturated fatty acid (e.g., stearic acid creates an extremely long induction period and the slowest oxidation rate; a single double bond would have an induction rate of 82 hours and the slowest rate of o; two double bonds lowers the induction bond further ~19 hours, with a much higher oxidation rate; three double bonds has an induction period of ~1.5 minutes with the highest oxidation rate)
222
Describe the propagation phase of lipid oxidation.
* Once the carbon radical is formed, it will immediately react with molecular oxygen to form an unstable fatty acid peroxyl radical (ROO\*) * This reaction is relatively fast and is the start of a chain reaction, where the peroxyl radical reacts with another fatty acid (by hydrogen abstraction) to form more peroxyl radicals * Forms hydroperoxides which are recognized to contribute to the off-odours and off-flavours associated with rancidity → very unstable and readily decompose to shorter chains which lead to subsequent reactions (secondary products of lipid oxidation)
223
What are the products of initiation and propagation?
Initiation = lipid radicals Propagation = hydroperoxide Secondary products = aldehydes, ketones, alcohols, small acids, alkanes
224
Describe the termination of lipid oxidation.
* The chain reaction continues until termination, which can occur by the donation of a hydrogen atom to the peroxyl radical from chain breaking antioxidants (TH), and by the reaction of the peroxyl radical and an antioxidant radical.
225
Discuss the secondary products of lipid oxidation.
Hydroperoxides undergo beta-scission **Malonaldehyde** → dialdehyde preferentially formed by autooxidation of fatty acids with three or more double bonds; odorless; very reactive; through cross-linking can bind proteins and denature them or nucleic acids and inactivate them Even at trace levels, malonaldehyde is an indicator of lipid oxidation (=TBA test)
226
What is hydrolytic rancidity?
Occurs from lipolysis (release of free fatty acids) by action of enzymatic lipases Released PUFA are oxidized by lipooxygenase or cyclooxygenase to form hydroperoxides or endoperoxides Enzymatic cleavage of hydroperoxides yield further breakdown products (secondary; flavours)
227
What is radiolytic rancidity?
Ionizing irradiation of fats; not natural Radiolytic products (dependent on FA composition) Chemical breakdown and generation of free radicals In presence of oxygen, irradiation accelerates autooxidation (free radicals generated will combine with oxygen to form hydroperoxides; their breakdown forms carbonyl compounds and free radicals; destruction of antioxidants)
228
What enzyme is present in veggies and plants that initiates hydrolytic rancidity?
Lipoxygenases
229
What are lipoxygenases?
* A family of iron-containing enzymes that catalyze the dioxygenation of polyunsaturated fatty acids and associated esters or acylglycerols to produce active hydroperoxides. Causes oxidative damage and destruction of vitamin A and carotenes * Activation: iron (ferrous - Fe+2) (oxidized) → iron (ferric - Fe+3) * Has a copper prosthetic group * May be prevented by blanching, pasteurization etc.
230
What are effects attributed to lipoxygenase activity? [4]
1. **Nutritional losses** * Oxidation of EFA (linoleic, linolenic, and arachnidonic acids) * Interaction with essential a.a. causes damage/loss of protein functionality 2. **Colour changes** 1. Bleaching of carotene or carotenoid destruction 2. Destruction of chlorophyll 3. Destruction of skin pigmentation in some fish products 3. **Flavour changes** 1. Production of off-flavours in frozen vegges and stored cereals 2. Off-flavour product is a cardboard-like flavour 3. Rancidity of meats 4. **Texture changes** 1. Loss of SS-SH balance of proteins and hydrophobic bonding of lipids in glutens, which contributes to reduction of flour dough quality
231
How do photosensitizers influence lipid oxidation?
Pigments in the lipid (e.g., chlorophyll, porphirin, myoglobin) convert triplet oxygen to singlet oxygen which will initiate oxidation reaction
232
How does temperature influence lipid oxidation?
The higher the temperature, the faster the reaction. Anisidine value is a measure of hydroperoxides (primary/initial product of lipid oxidation) At 50 degrees C, the end of the line indicates that the hydroperoxides have begun to decompose into secondary lipid oxidation products
233
How does water activity influence lipid oxidation?
* If too low, there is little reducing power to neutralize the hydroperoxides (aw = 0.1 - 0.2) * Inreased water activity accelerates oxidation reactions by solubilizing the catalyst, or swelling macromolecules to expose catalytic sites. * If too high, a dilution of the catalyst occurs to retard oxidation (aw = 0.75 - 0.85)
234
How does presence of antioxidants influence lipid oxidation?
* Prevents lipid oxidation by reacting with free radicals directly which breaks the chain reaction by either: * Decomposing peroxides (propagation phase) * Complexing with metal catalysts (initiation phase)
235
What are some natural antioxidants and synergists? [6]
Tocopherols (Fat soluble) Citric acid Ascorbic acid (water soluble) Lecithin Phenolic compounds Vitamin A (Fat soluble)
236
What is a free radical?
Molecules with one or unpaired electrons Unstable, thus reactive Reactive oxygen species
237
What are strategies for manipulating the prooxidative and antioxidative balance to maximize the oxidative stability of food? [5]
* Control generation of free radicals * Control availability of lipid oxidation catalysts * Inactivate oxidation intermediates and alter lipid oxidation breakdown products * Change in physical factors (e.g., surface area) * Control exposure to light and oxygen thru packaging
238
What are strategies for manipulating the pro-oxidative and anti-oxidative balance to maximize the oxidative stability of food? [5]
* Control generation of free radicals * Control availability of lipid oxidation catalysts * Inactivate oxidation intermediates and alter lipid oxidation breakdown products * Change in physical factors (e.g., surface area) * Control exposure to light and oxygen thru packaging
239
How does the control of free radicals maximize oxidative stability of food?
* Antioxidants bind to free radicals and form a more stable anti-oxidant radical thus blunting the reaction * Free radical scavengers react mainly with the peroxyl radicals (LOO\*) * Carry-through characteristics (BHA & BHT - food additives/synthetic anti-oxidants) * Regulations for use in foods (do not exceed 0.02%) * Necessary because natural antioxidants cannot survive food thermal processing
240
What are free-radical scavengers?
They have reducing activity, pro-oxidant sequestering activity, transition metal ion sequestering activity.
241
Give examples of free-radical scavengers.
**Hydroxyl (OH) containing compounds** * Often phenolic compounds (e.g., BHA, BHT, PG, TBHQ, natural plant phytochemicals). * Non-enzymatic antioxidants: * Tocopherol, ascorbic acid, beta-carotene, carnosic acid, ubiquinone
242
Rank the effectiveness of antioxidants.
Beta-carotene is the most effective singlet-oxygen quencher. Tocopherols work less effectively. BHA, BHT, TBHQ are also less effective but are allowed by FDA for use in foods.
243
Rank the effectiveness of antioxidants.
Beta-carotene is the most effective singlet-oxygen quencher. Tocopherols work less effectively. BHA, BHT, TBHQ are also less effective but are allowed by FDA for use in foods.
244
What does the relative effectiveness of antioxidants depend on?
* **Reduction potential** (FRS \> PUFA \< free radical) * FRS will donate the hydrogen to the radical more readily than the PUFA, therefore sparing the PUFA from oxidation. * Hydrophilic FRS are more effective in bulk oils than hydrophobic FRS. * Hydrophobic FRS are more effective in oil-in-water emulsions than hydrophilic FRS because solubility influences the phase partitioning of the FRS in the food system.
245
Why are hydrophobic FRS more effective in oil-in-water emulsions than hydrophilic FRS?
Solubility influences the phase partitioning of the FRS in the food system.
246
Hydrophilic FRS are less effective in bulk oils than hydrophobic FRS. True or False?
False. Hydrophobic FRS are MORE effective in bulk oils than hydrophobic FRS.
247
Hydrophobic FRS are more effective in bulk oils than hydrophilic FRS. True or False?
False. Hydrophobic FRS are LESS effective in bulk oils than hydrophilic FRS.
248
Hydrophobic FRS are more effective in oil-in-water emulsions than hydrophilic FRS. True or False?
True.
249
Hydrophilic FRS are less effective in oil-in-water emulsions than hydrophobic FRS. True or False?
True.
250
How can lipid oxidation catalysts be controlled to maximize oxidative stability of food? [3]
1. Control of prooxidant materials 2. Control of singlet oxygen 3. Control of hydrolytic activity (e.g., lipoxygenases)
251
How can pro-oxidants be controlled to maximize oxidative stability of food?
Transition metals are controlled by metal chelators or proteinaceous compounds (e.g., transferrin)
252
How can singlet oxygen be controlled to maximize oxidative stability of food?
Inactivated by presence of reactants that contain unsaturated groups, or by physical quenching (e.g., carotenoids)
253
How can hydrolytic activity of lipoxygenases be controlled to maximize oxidative stability of food?
Lipid oxidation catalysts (e.g., lipoxygenases) are active in plants and some animal tissues. Generates hydroperoxides from C18:2, n-6. Lipoxygenases are indirectly inhibited by phenolics which reduce iron in enzyme active site. Denatured by heat (e.g., blanching).
254
What are photoactivated sensitizers?
* Light activated sensitizers (e.g., chlorophyll, riboflavin, and heme-containing proteins) raise electrons to an excited state * Thus, promote oxidation by interacting with oxidizable substrate by transferring energy or excited electrons * _Result_ → produces free radicals or superoxide anion * Inactivated by carotenoids which absorb the energy.
255
What are the consequences of lipid oxidation breakdown products on food quality? [3]
1. Fatty acid oxidation causes a breakdown of secondary lipid oxidation products (e.g., aldehydes that evoke rancidity; e.g., head space volatiles) 2. Lipid oxidation products inactivate enzymes and causes oxymyoglobin oxidation leading to colour changes 3. Generation of these compounds will adversely affect the sensory and nutritional quality of foods.
256
What are sterols?
Sterols/steroid alcohols; synthesized endogenously from the precursor squalene. High molecular weight alcohols which are present in the **un-saponifiable** fraction of lipids Subgroup of steroids with a hydroxyl group in the 3-position of the A-ring.
257
What are plant sterols known as? Give examples.
Phytosterols Sitosterol (corn) Stigmasterol (soybean)
258
What is the principle sterol in animal and human body tissues?
Cholesterol
259
What is ergosterol?
Originally isolated from ergot, but can be obtained from yeast.
260
Cholesterol
261
Sitosterol (corn)
262
Stigmasterol
263
What is the concern with cholesterol and health?
* An increase in cholesterol deposition within hepatic cells also results in an increase in the serum LDL-cholesterol, an atherogenic lipoprotein. * Control of hypercholesterolemia is important for the prevention of atherosclerosis and coronary heart disease.
264
How may blood cholesterol levels be lowered to reduce atherosclerosis risk?
* Reducing sources of dietary cholesterol * Increasing amount of fibre in diet; interferes with bioavailability of dietary cholesterol * Consuming oils high in polyunsaturated fatty acids while reducing the intake of saturated fats * Plant products (e.g., flaxseed, peanuts) also contain cholesterol-like compounds, known as phytosterols, which are suggested to help lower serum cholesterol; compete with animal sterols for biosalts which are required to emulsify biosterols for absorption, which reduces the extent of animal cholesterol
265
Where are cholesterol oxidation products found?
* Cholesterol oxidation products have been identified in several processed foods including dried eggs, meat and dairy products, in fried foods, and heated fats.
266
What are the initial products of cholesterol oxidation?
Initial products are 7α- and 7β-hydroperoxides.
267
Discuss cholesterol oxidation.
* Initial products are 7α- and 7β-hydroperoxides. * Decomposition of the hydroperoxides produce the isomeric 7α- and 7β-hydroxycholesterols, cholesterol α- and β-epoxides, and 7-ketocholesterol. * Side-chain derivatization result in production of 20- and 25-hydroxycholesterols. * Cholesterol 3,5-diene, cholesta-3,5-dien-7-one and other ketones arise from elimination reactions.
268
Discuss the mechanism of cholesterol oxidation.
1. Cholesterol is initiated by a free radical or a trace metal ion to produce a allyl radical. 2. Allyl radical reacts with oxygen to form a peroxyradical. 3. The peroxy radical then further converts to a hydroperoxide. 4. The hydroperoxide is transformed into either the more stable products (alcohol radicals) 7-hydroxycholesterol or 7-ketocholesterol OR it can become an even more cytotoxic isomer called 5,6-epoxide radical (of which we are particularly concerned about for cholesterol oxidation)
269
Discuss cholesterol oxides in egg products.
Fresh egg yolk has no cholesterol oxides. Under storage conditions cholesterol oxides are generated.
270
Discuss the changes in cholesterol content in tallow heated to 155 and 190 degrees C.
Cholesterol disappears over time at these temperatures. The higher the temperature the faster the disappearance. The disappearance of cholesterol is correlated with the appearance of the oxidized products (not shown in graph).
271
Name three methods to measure lipid oxidation.
Peroxide value Anisidine value Thiobarbituric acid test
272
What is peroxide value?
* Peroxides are the **main initial products** of autooxidation. * Peroxides can be measured by their ability to liberate iodine from potassium iodine (iodimetry) or to oxidize ferrous to ferric ions (thiocynanate method). * The amount of iodine liberated from KI by oxidative action of peroxides present in the oil is determined by titration in a biphasic system with Na2S2O3.
273
Describe the thiobarbituric test.
* Most frequently employed method; measures **secondary products.** * Substrate is malondialdehyde (MDA), a major breakdown product of lipid peroxides * MDA derives from beta-cleavage of endocyclization of fatty acids hydroperoxide and reacts with thiobarbituric acid (TBA) to give a pink and fluorescent chromogen that is measured by colorimetry or fluorimetry. * This method lacks specificity for MDA since all compounds with reducing activity will react with TBA. * The TBA test is often useful for comparing samples of a single material at different stages of oxidation.
274
What is smoke point?
* The temperature at which an oil gives the first trace of smoke when heated at a specific rate. * A high smoke point is desirable for frying fat. * The smoke point will vary depending on the molecular weight of the fat. * A good frying oil will have a smoke point of 420-450 degrees F.
275
Discuss deep fat frying.
Frying in hot oil under very high temperatures; thermal lipid oxidation is assured. During frying, the sensory and nutritional quality of the frying oil change. The increased temperature increases the solubility of oxygen; thus, making greater access between the oxygen and the lipid component. In addition there are dynamic changes with water with release from the food sample and the dehydration associated with this; hydrolysis increases susceptibility to lipid oxidation
276
Describe oxidation as it occurs during deep fat frying.
During deep fat frying, oxygen is introduced into the oil as the food enters the hot oil causing oxidation. Oxidation products include hydroperoxides, aldehydes, ketones, acids, hydrocarbons, and polymeric compounds.
277
Describe dehydration as it occurs during deep frying.
Moisture is released from the frying food into the frying oil and the food absorbs the oil. As the food absorbs the frying fat, the food lipids and pigments are solubilized and released into the frying oil.
278
Describe hydrolysis of triglycerides as it occurs during deep fat frying.
* Excessive heat and presence of moisture in the frying oil results in hydrolysis of triglycerides yielding free fatty acids, glycerol, mono- and di-glycerides. * The volatile degradation products are released from the oil with the steam as smoke.
279
Describe polymerization as it occurs during deep fat frying.
* Occurs with prolonged and high temperature frying. * Leads to formation of **Diels-Alder** reactions that include the formation of polymers as the reaction products condense. * Products include dimers and cyclic compounds * Polymerization leads to changes in molecular weight, viscosity, and heat-transfer efficiency of the oil.
280
What are Diels-Alder reactions?
* Occurs with prolonged and high temperature frying. * Includes the formation of polymers as the reaction products condense * Products include dimers and cyclic compounds. * Leads to changes in molecular weight, viscosity, and heat-transfer efficiency of the oil.
281
What factors affect deep fat frying? [4]
**1) Temperature and frying time** Optimal is 150 to 180˚C (300 – 350˚F) **2) Fryer type** _Batch_: a space in which a product is lowered into the oil, e.g. french fries. (greater access to air) _Continuous_: a conveyor belt transports the product through the cooking oil bath, e.g. doughnuts (can minimize uptake of oxidation products into food product by reducing contact time) **3) Source of oil** _Chemistry_: with frying, fatty acid content increases, iodine value decreases, and refractive index changes. _Physical_: viscosity changes, development of darker colour, decrease in surface tension, and increase tendency to foam. **4) Source of food** _Properties_: release of lipids into frying oil. Bidirectional transfer of free fatty acids will influence the susceptibility of thermal oxidation of the oil. _Chemical_: presence of the food contributes to Maillard reaction.
282
Why do crude oils and fats derived from plant and animal sources require processing?
Processing is required to remove substances such as fatty acids, phospholipids, carbohydrates, proteins, degraded products, water pigments (carotenoids and chlorophyll), as well as other lipid oxidation products. Removal prevents from undesirable flavour, colour, and keeps quality of lipid source intact.
283
Processing vegetable oils are designed to remove undesirable substances. What processes are included?
Settling and degumming Neutralization Bleaching Deodorization
284
What is winterization?
Removal of high-molecular weight hydrocarbons during refining of vegetable oils
285
Describe the steps in fat and oil processing.
**Crude oil** (flax, sunflower, soybean etc.); oil systems with at least 8-10% oil content → **degumming** (involves removing components that would otherwise interfere with further processing such as lecithin or phytosterols) → **neutralization** (removal of free fatty acids associated with soap stock, a product of the previous reactions) → **washing & drying** → **winterisation** (specific lower temperatures to induce crystallization of the lipids in order to remove high molecular weight hydrocarbons like waxes; thus, providing a better textural oil) → **bleaching** (remove pigments that can bring about photooxidation) → **deodorisation** (bleaching step must be deodorised using steam; produces a fatty acid distillates; natural tocopherols are lost and must be added back, that is, fortified in order to provide some stability after the process) → **refined oil**
286
What is hydrogenation?
Involves the addition of hydrogen to double bonds in the fatty acid chains. It is commercially used for the production of margarine, salad oils, shortening and cooking fats.
287
What is the purpose of hydrogenation?
1. To allow conversion of liquid oils into semisolid or plastic fats more suitable for specific applications 2. To improve the oxidative stability of the oil.
288
What are the requirements for hydrogenation processing?
1. Oil, hydrogen gas and nickel catalyst are mixed together in a reactor. 2. The starting oil must be refined, bleached, low in soap, and dry. 3. The hydrogen gas must be dry and free of sulfur, CO2, or ammonia.
289
Describe the process of hydrogenation. What does selectivity refer to?
* The oil is first mixed with the catalyst. * Heat to 140-225 degrees C. * Expose to hydrogen gas under pressure of 60psi. * Mixture is agitated to enhance the dissolving of hydrogen to uniform catalyst with the oil and to help dissipate the heat of the reaction. * Selectivity refers to the rate of hydrogenation of the more unsaturated fatty acids as compared with that of less unsaturated acids. (e.g., linolenic acid compared to linoleic)
290
Why is hydrogenation not typically used?
Trans fat formation Governments have regulations that do not allow foods that are high in trans fatty acids to carry claims for low in saturated fatty acids. Information on trans fatty acids in nutritional information label should be included.
291
What is interesterification?
* To create fats with no trans fatty acids but with improved functionality. * The physical characteristics of a fat are affected not only by the nature of the constituents fatty acids (e.g., chain length and unsaturation) but also their distribution in the triglycerol molecules * Interesterification involves rearranging the fatty acids so they become distributed randomly among the triglycerol molecule.
292
Describe the process of interesterification.
* Accomplished by heating fat at relatively high temperatures (\<200degreesC) for long periods. * Catalysts are used to allow the reaction to be completed in shorter times (e.g., 30 mins) and at lower temperatures (as low as 50degrees C) * The process results in the shuffling of fatty acids within a single molecule and among triacylglyceride molecules until an equilibrium is achieved in which all possible combinations are formed. * After esterification, the catalyst is inactivated by addition of water, or acid, and products are removed.
293
What are applications of interesterification?
* Restructuration of desirable lipids that meet essential fatty acid dietary requirements (achieved by temperature control; done automatically based on the fact that different chain lengths and degree of unsaturation changes the recrystallization temperature) * Production of new medium chain triglycerides for specific purposes (e.g., lower caloric density) * Its greatest application is the manufacture of shortenings * Salad oils, high-stability margarine blends, hard butter * Reduction of the content of linolenic acid (C18:3 an EFA) in soybean oil, which is responsible for bitterness in soybean oil
294
How is lipid composition measured?
Iodine value/number Ultraviolet (UV) spectrophotometry Chromatographic methods
295
How are primary lipid oxidation products measured?
Peroxide value (PV) Ultraviolet (UV) spectrophotometry Chromatographic methods
296
How may secondary lipid oxidation products be measured?
Anisidine value Thiobarbituric acid (TBA) test Total and volatile carbonyl compounds Fluorescence Rancimat method Sensory evaluation Chromatographic methods
297
How may oxidative stability be measured?
Active oxygen method
298
What is anisidine value (AV)?
Aka P-Anisidine value (PAV) Measures aldehyde & ketone levels in oil or fat (especially sensitive to unsaturated) Aldehyde/ketone + P-anisidine → schiff bases (yellow; absorb @350nm)
299
What are TBARS? Why are they relevant?
TBA-reactive substances. TBA test lacks specificity for MDA since all compounds with reducing activity will react with TBA. TBARS react with TBA.
300
Chemicals which are introduced purposely into foods to aid in processing, as a preservative, or to improve quality of the food system, are called intentional additives. True or False?
True.
301
Intentional food additives must be classified as GRAS before approval. True or False?
True
302
Acids/acidulants are incorporated in food systems to impart flavour and tartness. True or False?
True
303
Acids/acidulants are incorporated into food systems to give antimicrobial activity. True or False?
True
304
Acids/acidulants are incorporated into food systems to provide buffering and leavening action. True or False?
True
305
Several acids, due to metal chelating activity, are used with antioxidants to work synergistically to prevent rancidity of fat. True or False?
True
306
Acidulants are used in gel-like products, such as jams and jellies to provide a pH that is optimal for gel character and strength. True or False?
True
307
Sequestrants are metal-chelating agents used to stabilize colour, flavour, and texture properties of foods. True or False?
True
308
Free metal ions are reactive agents that can lead to deterioration of food quality. True or False?
True
309
EDTA is equally effective to inhibit Cu- or Fe-catalyzed chemical reactions. True or False?
True
310
Citric acid is used only as an acidulant to prevent oxidation reactions. True or False?
False. Citric acid is used as both an acidulant _and_ a metal-chelating agent to prevent oxidation reactions.
311
BHA and BHT are natural antioxidants soluble in fats and oils. True or False?
False
312
BHA and BHT are heat sensitive. True or False?
False
313
Cereals, oilseeds and vegetables all contain carotenoid antioxidants. True or False?
False.
314
Emulsions are heterogenous systems, where one immiscible liquid intimately disperse in another, one which: in the form of droplets with a diameter generally over 0.1u True or False?
True
315
Emulsions have minimal stability by themselves and can lead to coalescence. True or False?
True
316
An O/W emulsion has the oil in the dispersed phase and the water in the continuous phase. True or False?
True
317
Surface active agents (i.e., surfactants) are termed emulsifiers, which act to reduce the interfacial tension between air-liquid and liquid-liquid interfaces. True or False?
True
318
Emulsifiers possess hydrophilic and nonpolar/lipophilic properties. True or False?
True
319
The relative sizes of the hydrophilic and lipophilic sections of an emulsifier molecule determine its emulsification behaviour. True or False?
True
320
How is an emulsifier selected?
We use the HLB (hydrophobi-lipophile balance) expression.
321
The HLB expression is… [2]
* a numerical expression for relative simultaneous attraction of emulsifier for water or oil * an indication on how an emulsifier will behave but _not_ how effective it is
322
Low HLB values form W/O emulsions. True or False?
True
323
Low HLB values form O/W emulsions. True or False?
False.
324
High HLB values form O/W emulsions. True or False?
True.
325
High HLB values form W/O emulsions. True or False?
False.
326
Foods may contain natural emulsifiers such as phospholipids, e.g., lecithin. True or False?
True
327
If an oil-soluble dye is added to an emulsion and the colour spreads rapidly, the emulsion is: W/O? or O/W?
W/O
328
Most oils are poor conductors of electricity, so therefore a W/O emulsion will demonstrate low electrical conductivity properties. True or False?
True
329
The amount of emulsifier required sharply increases with decreasing particle size of the emulsion droplet. True or False?
True
330
Amphiphilic primary antioxidants with high HLB are more effective in bulk oils. True or False?
True
331
Non-polar antioxidants with low HLB are more active in polar emulsions. True or False?
True
332
Ascorbic acid is more effective in bulk oil than corresponding nonpolar alkyl esters. True or False?
True
333
Name 2 ways buffer solutions may be formed.
1. A weak acid and a salt of the acid's conjugate base 2. A weak base and a salt of the base's conjugate acid
334
Phosphates are preferred over citrates for tartness. True or False?
False. Citrates are preferred over phosphates for tartness modification since they yield smoother sour flavours.
335
Give 3 examples of additives commonly used for pH control and tartness.
Sodium salts of gluconic, acetic, and phosphoric acids.
336
What are the functions of acidulants used as food additives? [4]
1. Buffering 2. Preservation 3. Flavour enhancement 4. Leavening
337
What are the effective buffering ranges for citric acid and sodium citrate (salt)?
2.1 - 4.7
338
What are the effective buffering ranges for acetic acid and sodium acetate (salt) ?
3.6 - 5.6
339
Describe the use of acidulants for flavour enhancement.
Evoke tartness Each acid has varying degrees of acidity.
340
Define: pH
Logarithm of the concentration of free protons, expressed with a positive sign.
341
Define total acidity.
Proton equivalence (# of protons or hydrogen ions that the organic acids would contain if they were undissociated)
342
Define titratable acidity.
protons recovered during a titration with a strong base to a specific endpoint Not synonymous with total acidity Easier to measure than total acidity. Titratable acidity \< Total acidity
343
Titratable acidity \> Total acidity True or False?
False. Titratable acidity \< total acidity
344
Total acidity is easier to measure than titratable acidity. True or False?
False. Titratable acidity is easier to measure.
345
Why do we measure titratable acidity?
We measure titratable acidity to give an idea about the potential of the acidulant to function during changes in buffering capacity of the food system.
346
pH and titratable acidity (TA) are both measures of acidity. True or False?
True.
347
What is the difference between pH and titratable acidity?
* pH measures only those protons that are free in solution and not associated with salts or proteins, so it is a better process control tool (e.g., important for quality parameters such as microbial control, sour taste, and protein functionality (the pH will influence moisture, mineral contents, texture, and flavour) * TA measures both free protons and those associated with organic acids and proteins. * Example → the pH of fresh milk ranges between 6.6-6.8, which gives a true indication of the acid development. The TA will vary with initial milk composition, milk heat treatments, and the procedure used to standardizew milk composition (e.g., if you remove protein, like whey, you change the buffer capacity of milk, thus TA changes)
348
Describe the use of acidulants for preservation. [2]
A low pH results in: * Saturation of cell walls with hydrogen ions, thus limiting cation transfer in microbes. * Penetration of cell wall by hydrogen and changes in intracellular pH and enzyme function
349
List 5 common acidulants.
Fumaric acid Succinic acid Malic acid Tartaric acid Citric acid
350
What is fumaric acid used for?
2 pK values Used to preserve shelf-life of dehydrated food products. Used with benzoic acids.
351
What is succinic acid used for?
2 pK values Derived from fumaric acid; used in dough making; has use as an emulsifier as well (monoester with glycerol)
352
What is malic acid used for?
2 pK values Used as a monoester with fatty alcohols in frying fats and oils
353
What is tartaric acid used for?
2 pK values Has a hard taste; utilized in fruit juices and sour candies.
354
What is citric acid used for?
3 pK values Utilized in fruit juice, ice cream, jelly, vegetable canning and milk. Suppresses enzymatic browning as it is a synergist to antioxidants.
355
Where are the common food sources of the following acids: Citric Malic Oxalic Acetic Lactic Carbonic
Citric → lemon, lime Malic → apple Oxalic → rhubarb Acetic → vinegar Lactic → sour milk Carbonic → soft drink
355
Where are the common food sources of the following acids: Citric Malic Oxalic Acetic Lactic Carbonic
Citric → lemon, lime Malic → apple Oxalic → rhubarb Acetic → vinegar Lactic → sour milk Carbonic → soft drink
356
Why is citric acid an especially useful acidulant?
Dual effect Citric acid: pK1 = 3.09; pK2 = 4.74; pK3 = 5.41 * suppresses enzymatic browning * Synergistic activity with antioxidants.
357
Citric acid: pK1 = 3.09; pK2 = 4.74; pK3 = 5.41 At pH = 2.2, what is the ionic form of citrate?
Citric acid predominates in the most protonated form (citric acid)
358
Citric acid: pK1 = 3.09; pK2 = 4.74; pK3 = 5.41 At pH = 7, what ionic form of citrate predominates?
The citric acid will lose all its protons and occur predominantly in the citrate-3 form.
359
What is the Henderson-Hasselbach equation and what is it used for?
To determine the dominant form of an acid at any pH. pH=pKa+log[A-]/[HA]
360
What are sequestering agents?
Chelating agents/ligands that either precipitate the metal or suppress its reactivity. May be organic (e.g., citric acid, tartaric acid, sorbitol (i.e., long chain alcohols)) or inorganic (e.g., phosphates).
361
How may a formation of metal complex be expressed?
M: metal ion L: ligand ML: metal-ligand complex k = stability of complex
362
Why do we want to chelate transition metal ions?
They are effective catalysts of oxidation reactions that lead to rancidity, discolouration, and undesirable textural changes in food.
363
Give 3 examples of transition metals which are effective catalysts of oxidation reactions.
Iron Copper Aluminum
364
What is the Haber-Weiss cycle? What are the resulting products?
Iron participates in the Haber-Weiss cycle in which ferrous ion reduces oxygen to superoxide anion (O-2). The resulting products are H2O2 and O2 (these feed into the Fenton reaction) This is a bidirectional reaction.
365
What is the Fenton reaction?
The combination of ferrous ion with hydrogen peroxide (H2O2). The Fenton reaction produces highly reactive hydroxyl radical which oxidizes most food constituents.
366
What is EDTA?
Ethylenediamine tetraacetic acid Very strong capacity to sequester iron. It has 6 possible coordination interactions (3 on each side of the molecule) This may be sufficient to sequester copper, but it's not 100% effective for iron.
367
Complexation of transition metals by soluble chelators like EDTA will preclude iron from being reactive. True or False?
False. EDTA has the capacity to interact with 6 coordination sites. Effective at sequestering many ions. It's not 100% effective when it comes to iron. Iron is chelated to EDTA, but iron has 7 coordination sites, so 1 is not occupied by the EDTA. Thus, the 7th site (i.e., aquasite) is open for reactions. So EDTA is not 100% effective although it will significantly suppress the Haber-Weiss cycle and Fenton reaction. The 7th site left open is particularly reactive since it is more soluble.
368
Describe the limitation of EDTA to chelate iron. [2]
* Iron chelated to EDTA has seven coordination sites, one of which is occupied by water, and therefore available for reduction-oxidation reactions. * The high solubility of Fe3+-EDTA and the free coordination sites promote oxidative damage by increasing both the solubility and oxidation-reduction potential of iron.
369
How many coordination sites does citrate have?
3
370
How many coordinating sites does iron have?
7
371
Ascorbate reduces the uptake of ferrous iron in humans and animals. True or False?
False! Ascorbate **enhances** the uptake of ferrous iron in humans and animals, attributable to the chelation and reducing power of ascorbate.
372
Describe the importance of ascorbate as it relates to the Haber-Weiss cycle and the Fenton reaction.
Ascorbate is a strong reducing agent (Fe3+ → Fe2+), that contributes to the Haber-Weiss cycle and the Fenton reaction in producing hydroxyl radical. Thus, at low concentrations ascorbate can act as a prooxidant. At high concentrations, ascorbate will act as an antioxidant because there is sufficient ascorbate to sequester the hydroxyl radical that is produced from the Fenton reaction.
373
What are the 4 classifications of antioxidants?
1. Free radical terminators (chain breakers) → involves propagation (scavenge the hydroxy-radical with tocopherol) 2. Reducing agents → reduce radicals and regenerate the lipid antioxidants which act as hydrocarbons 3. Oxygen scavengers → beta-carotene is very good at scavenging superoxide ion 4. Chelating agents → ties up free metal ions that can initiate lipid oxidation.
374
What are antioxidants? [2]
* A substance used to preserve food by retarding deterioration, rancidity, or discolouration due to oxidation reactions. * Antioxidants slow down the effects of oxidation and preserve the nutritional and organoleptic qualities of the food product.
375
How do free radical terminators function?
Mitigate the free-radical chain reaction (e.g., vitamin E) * Retard the free-radical chain reaction by donating hydrogen from their phenolic hydroxyl group. * These antioxidants are: * More easily oxidized than other substances * Once oxidized they are relatively stable
376
Give examples of free radical terminators (antioxidants). [6]
* Butylated hydroxyanisol (BHA) * Butylated hydroxytoluene (BHT) → BHT and BHA often used together due to synergistic effects * Tertiary butylhydroxyquinone (TBHQ) → most effective synthetic antioxidant often used in preventing oxidation of frying oils * Propyl gallate (effectiveness decreases at higher temperatures) * Vitamin E (tocopherols) * Carotenoids (Beta-carotene)
377
How do reducing agents and oxygen scavengers work as antioxidants?
They function by transferring hydrogen atoms to radicals.
378
Give examples of reducing agents and oxygen scavengers. [5]
* Ascorbyl palmitate * Sulfites * Ascorbic acid * Glucose oxidase * Erythrobic acid
379
Chelating agents are antioxidants. True or False?
False. They are not true antioxidants, but they are usually used in combination with true antioxidants.
380
Give examples of commonly used chelators with antioxidant function. [3]
Citric acid EDTA Phosphates
381
Citrate is more effective at sequestering copper than pyrophosphate. True or False?
False.
382
How do chelating agents assist in antioxidant function?
The unshared pair of electrons in their molecular structure promotes the chelating/sequestering effect with the ions.
383
Phosphates are less effective than citrate at chelating copper. True or False?
False
384
EDTA is more effective than both citrate and pyrophosphate at sequestering iron or copper. True or False?
True
385
What is an emulsion?
* An example of a dispersed system, usually characterized by 2-immiscible liquids. Other forms include foams, aerosols, and suspensions. * Consist of an outer phase (continuous) and an inner (dispersed) phase.
386
What is an oil in water emulsion? Give examples.
When the outer phase is water (and inner is oil), we refer to it as an oil in water (o/w) type emulsion. e.g., mayonnaise, ice cream (milk)
387
What is a water in oil emulsion? Give examples.
When the outer phase is oil (and inner is water), we refer to it as a water in oil (w/o) type emulsion. e.g., salad dressing, margarine
388
What does visual appearance of an emulsion depend on?
Droplet diameter ## Footnote e.g. 1micrometer or greater = milky-turbid…. When the diameter is very, very small, such as close to light wavelength (10-5 cm) it is optically clear & micro/nano emulsion
389
Emulsifiers act to prevent coalescence. True or false?
True
390
What is Ostwalk Ripening?
Results in the breaking of an emulsion.
391
What factors influence the stability of O/W emulsions? [7]
1. Chemical structure of lipids 2. Oxygen concentration 3. Antioxidants 4. Interfacial characteristics 5. Droplet characteristics 6. Aqueous phase components 7. Ingredient quality
392
What are emulsifiers?
Agents that can decrease the surface tension at the interface of two immiscible phases (e.g., w/o or o/w) Amphiphilic nature of these molecules are responsible for their characteristic surface active properties.
393
What are the most commonly used food emulsifiers?
Esters of fatty acids; mono- & di-glycerides.
394
Give examples of naturally occurring emulsifiers.
Ionic (proteins, phospholipids like lecithin)
395
Give examples of synthetic emulsifiers.
Ionic (stearyl-2-lactylate) Non-ionic (mono/di-acylglycerols; with esters (citric, lactic, tartaric; sorbitol; saccharose fatty acid esters)
396
Emulsifiers are GRAS and restricted to specific applications and usage levels according to the FDA (require regulatory approval). True or False?
True
397
What is the hydrophilic-lipophilic balance (HLB) system? [3]
* Indicates the kind of emulsion for which the emulsifier is best suited * Emulsifiers with low HLB values tend to be oil soluble and are used to prepare w/o emulsions. * High HLB values shows a water-soluble emulsifier and then will be effective in preparing o/w emulsions
398
What is the phase inversion temperature (PIT) system? [3]
* Method to select emulsifier * Useful in relating the complex temperature-dependent phase behaviour of emulsifiers * As the temperature increases, non-ionic emulsifiers change from being preferentially water soluble to oil soluble.
399
Describe margarine as an emulsion. Describe which emulsifiers are used.
W/O * Monoglycerides, diglycerides, and lecithin * Water droplets coated with emulsifiers are important for minimizing the potential of microbial contamination and improving stability during storage. * All emulsifiers improve the consistency and creaming properties of the margarine.
400
How do monoglycerides promote emulsification?
By reducing interfacial tension between the oil and water phases when combined.
401
Most food systems exhibiting creaminess characteristics are w/o emulsions. True or False?
False! Most food systems exhibiting creaminess characteristics are o/w emulsions
402
What sensations are associated with O/W emulsions?
Uniform Smooth Creamy
403
What does thickened liquid viscosity of the continuous phase of o/w emulsion do?
Plays a significant role in perception of creaminess
404
What does increasing the oil content in emulsion give rise to?
A logarithmic increase in viscosity.
405
Describe the application of emulsifiers in bakery products. [3]
* Emulsifiers extend the shelf life or strengthen the dough by forming water insoluble inclusion complexes with the amylose fraction of starch * Complexes retard starch recrystallization/retrogradation * Emulsifiers interact with the proteins of yeast-raised wheat dough, shows better retention of carbon dioxide produced during leavening; hence giving a product increased volume and finer texture.
406
Describe the application of emulsifiers in cake batters.
* Emulsifiers function as aerating agents, speeding up the whipping rate of batter, providing a finer distribution of air cells and improving the tenderness of the cake by retarding starch gelatinization.
407
BHT/BHA more effective in emulsions than bulk oils. True or False?
True.
408
Tocopherol isomers are more effective in emulsions than bulk oils. True or False?
True.
409
Bulk oils have a low surface-volume ratio (LSV) and do not represent high surface-volume ratios (HSV), typical of emulsions, micelles and biological membranes. True or False?
True
410
Polar antioxidants, amphiphiles of high HLB, tend to be more active in bulk oils (e.g., low surface/volume; non-polar medium) True or False?
True.
411
Non polar antioxidants with low HLB tend to be more active in polar lipids and polar emulsions (e.g., high surface/volume HSV) True or False?
True.
412
O/W emulsions, in contrast to bulk oils, are better protected from oxidation by polar antioxidants than nonpolar ones. True or False?
False. O/W emulsions, in contrast to bulk oils, are better protected from oxidation by nonpolar antioxidants than polar ones.
413
Ascorbic acid has higher antioxidant efficiencies in bulk oil and lower efficiency in emulsions. True or False?
True.
414
What is the polar paradox theory?
The paradoxical behaviour of antioxidants in different media.
415
What is the higher effectiveness of nonpolar antioxidants in O/W emulsions attributable to?
Greater affinity for the oil-water interface
416
Antioxidants with low HLB are mainly concentrated where…?
At the oil-water interface forming a protective membrane around the lipid droplet
417
Polar antioxidants are mostly dissolved in the aqueous phase in O/W emulsions True or False?
True
418
Free radicals are scavenged by lipophilic antioxidants at the interface of O/W emulsions before they can cross the droplet membrane and enter the lipid phase. True or False?
True
419
Polar antioxidants are more effective where?
In less polar media (e.g., bulk oils)
420
Non-polar antioxidants are more effective where?
In polar media (e.g., O/W emulsions)
421
Describe antioxidants in bulk lipids (LSV). *Understanding the polar paradox*. [6]
* Oil/air interface → the site where oxidation is initiated and propagated to the inner parts of the oil * Partially fat soluble, polar antioxidants orient themselves at the oil-air interface where surface oxidation occurs. * BUT: bulk oil contains micro-nano-water environments from atmospheric moisture * Hence, evidence supports the hypothesis that the association of colloids are the site of lipid oxidation in bulk oils * Polar antioxidants are preferentially located at the interface of the colloid (e.g., the oil-water interface) * Non-polar antioxidants are dissolved in the lipid phase.
422
Describe antioxidants in emulsions (HSV). *Understanding the polar paradox*. [7]
* A heterogenous system (emulsified matrix in foods) * O/W → lipid droplets; continuous aqueous phase and the O/W interface * Pro/Anti-oxidants partition into these 3 phases depend on solubility and surface activity (structure and polarity) * Nonpolar antioxidants have a higher capacity in O/W due to greater affinity for the oil-water interface * Nonpolar antioxidants concentrate in the O/W interface, forming a protective membrane around the lipid droplet, while polar antioxidants are dissolved in the aqueous phase. * Free radicals are scavenged by the lipophilic antioxidants at the interface before they cross the droplet membrane and enter the lipid phase * Lipophilic antioxidants (e.g., BHA, Toc-isomers) are most effective in O/W emulsion
423
How does the mechanism of action of the antioxidant influence the polar paradox?
* Influences activity in multiphase media due to: * Prevent or retard initiation (sequester, quench initiators) → polar antioxidants inhibit initiation of oxidation at interface more ffectively than nonpolar antioxidants in the lipid phase * Breaking propagation chain → non polar antioxidants chain-breaking more efficient to inhibit propagation of oxidation in the lipid phase (where nonpolar oxygen molecules are preferentially dissolved)
424
How does the concentration of the antioxidant influence the polar paradox?
Effects the polarity-effectiveness relationship and the polar paradox may only be effective over certain concentration ranges. Interfacial phenomenon dominates over the solubility issue.
425
How does the molecular size of the antioxidant influence the polar paradox?
Mobility of the antioxidant in the multiphase system is an issue. Bulky structures (e.g., long alkyl chains) have low mobility due to steric hindrance. Mobility equates with diffusibility
426
Describe why oxygen content is important for understanding emulsion stability.
Oxygen is 3 times more soluble in oils than water. Rate of diffusion of oxygen through the aqueous phase is a rate-limiting step at low oxygen concentration. High oxygen concentration → rate of diffusion through aqueous phase is very fast.
427
Describe which factors are most important to consider for primary oxidation (in regards to emulsion stability).
Polarity → nonpolar antioxidants reside in the oil droplet or at the oil-water interface; readily interact with hydroperoxides. Electrical charge → dependent on pH and charge of the surfactant; ionizable groups may alter affinity for interface
428
Describe what factor is most important for secondary oxidation (in regards to emulsion stability).
Metal chelators are most important (they prevent metal redox cycling, form insoluble metal complexes; occupy metal coordination sites; give steric hindrance between metals and lipids)
429
Describe the droplet characteristics important in understanding emulsion stability. [3]
* Concentration of oil droplets in emulsion increases → more lipids are oxidized * Size → the rate of oxidation increases as the size of oil droplets decreases * Physical state → rate of lipid oxidation is slow when the fat is crystalline versus fluid.
430
The rate of lipid oxidation increases as the size of oil droplets increases. True or False?
False. The rate of lipid oxidation increases as the size of the oil droplets decrease.
431
The rate of lipid oxidation is slower when the fat is fluid versus crystalline. True or false?
False. The rate of lipid oxidation is slower when the fat is crystalline versus fluid.
432
Describe primary antioxidants.
Synthetic → BHA, BHT (highly effective in controlling lipid oxidation) Natural → high price, tastes and colours limited their utilization in the industry
433
Describe secondary antioxidants.
Chelators → chelating irons to retard lipid oxidation, however it can also have counter effect.
434
Limiting exposure of oxygen to the emulsion (e.g., vacuum packaging or nitrogen packaging) preservers emulsions. True or False?
True.
435
The presence of even small amounts of transition metals in an emulsion will accelerate production of lipid oxidation by promoting breakdown of hydroperoxides. True or False?
True. Use ingredients that have low transition metal concentration, or add substances that chelate and inactivate the transition metals.
436
Prevention of the generation of pro-oxidants (or inhibition of their activity) can be achieved by…?
Addition of primary / secondary antioxidants.
437
Prevention of the generation of pro-oxidants (or inhibition of their activity) can be achieved by…?
Addition of primary / secondary antioxidants.
438
What is a food colourant? And why is it important? [3]
* A food colourant improves food acceptability by increasing attractiveness * Colour has an indirect effect on nutritional perception. * Consumers perceive a richly coloured food to be more nutritious and flavourful.
439
Describe synthetic colourants. [4]
* Used since 1856 * Few are FDA approved * Associated with negative connotation * E.g., FD&C blue No. 1; FD&C red No. 40, FD&C Yellow No. 5.
440
Describe natural colourants. [4]
* Used since antiquity * Preferred by consumers * Patented * E.g., Annato (orange-red), saffron (orange, yellows), paprika (orange), anthocyanins (blues, purples), carotenoids (reds), curcumin (yellows, oranges)
441
Describe anthocyanin as a food colourant. [3]
* Anthocyanins are natural water-soluble pigments responsible for the attractive red, purple, and blue colours of many flowers, fruits and vegetables. * e.g., grapes, berries, red cabbage, apples, and wine. * Sensitive to pH change, being reddest in strongly acidic conditions and become more blue as the pH rises * *Enter → acidulants*
442
Anthocyanins become more red as pH rises. True or False?
False. Anthocyanins are reddest in strongly acidic conditions and become more blue as pH rises.
443
Discuss problems associated with use of anthocyanins. [2]
* Stability → react with ascorbic acid, metals, sugars, oxygen, light, and enzymes; results in production of polymers and degradation products * Sensitivity to pH → decolorize at values above 4; limits their use as colourants in neutral and basic food systems.
444
The intensity of sourness and ability to reduce pH vary among the organic group of acidulants. List in decreasing order of activity.
Fumaric \> Tartartic \> Malic \> Acetic \> Citric \> Lactic FTMACL (Featuring macklemore)
445
Why does lipid oxidation occur rapidly in oil-in-water emulsions?
The large surface area that facilitates interactions between lipids and water soluble prooxidants.