Meat Processing Flashcards

1
Q

Collagen

A

Most abundant protein in multicellular animals
Extra-cellular glycol-protein organised into fibres
High tensile strength
Stress and load bearing

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2
Q

Collagen structure

A

Triple helix
33% glycine
15-30% proline
Sugars are bound to amino acid residues

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3
Q

Collagen synthesis

A
Polypeptide synthesis
Hydroxylation of lysine and proline
(Needs vitamins C)
Glycolysation 
Triple helix forms
Secrete from cells in soluble form
Mature into fibre bundles
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4
Q

Hydroxylation

A

Peptide chain formation

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5
Q

Glycosylated

A

Forming a triple helix

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6
Q

Hydroxylysine

A

Cross link

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7
Q

Collagen Degradation

A

When heated to 60 degrees collagen fibrils are degraded to constituent molecule
Forms sol in water

Most stable below 30 degrees

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8
Q

Myoglobin

A

Myoglobin is a haem protein
Absorbs oxygen from blood and stores in muscle
When muscle needs more O2 it released from myoglobin

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9
Q

Myoglobin and cooking

A

When myoglobin is heated it denatures
Changes texture and colour of muscle
Beef most tender if heated to 65 degrees

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10
Q

Purpose of curing meat

A

Store meat at ambient temperature

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11
Q

Curing meat process

A

Immersed in brine
24% NaCl
0.3% NaNO3
0.1% NaNO2

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12
Q

NaCl and curing meat

A

2-6% in final product
Increases water holding capacity of cells
Reducing water activity
Inhibit microbial growth

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13
Q

NaNo3 and curing meat

A

Added as additional preservative

When O2 is low it can transfer NO3 to NO2

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14
Q

NaNO2 and curing meat

A

Active curing agent
Strong oxidant
Inhibits microbial growth of anaerobic bacteria

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15
Q

How does NaNO2 inhibit microbial growth

A

Oxidises Deoxymyoglobin to make metmyoglobin
Metmyoglobin reacts with nitrite to nitrosyl myoglobin
Nitrite breaks down to produce NO
NO forms with nitrite which may react with non-haem protein to form nitroso derivatives (N-nitrosamines)

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16
Q

Cancer risk and cured meat

A

Concerned about N-nitrosamines
But have developed a way to minimise there formation.
Reduction of the use of nitrite and nitrate and start using increased amount of ascorbic acid
But risk of N-nitrosamines is less than anaerobic bacteria that could grow in meat

17
Q

Salt Detection

A

Ion channel that allows Na+ ions to enter cell generate taste
ENaC

18
Q

Salt taste

A

Na+
K+ and Li+
Enhances other tastes
Prevent sodium deficiency but too much has aversive taste

19
Q

Muscle protein structure

A

Thick and thin filaments organised into repeating units called sarcomeres
Light and Dark Zones with ends that overlap

Light band - hexagonally arranged thin filaments
Dark zone contain only hexagonally arranged thick filaments

20
Q

Muscle contraction

A

Electric stimulus from nerve fibre
Release Ca2+ into muscle
ATP bind to thick filament
Ca2+ binds to thin filament exposing a binding site
ATP hydrolysis -> Conformational change, pulls thin filament toward centre of sarcomere
ADP+Pi released
Muscle contracts

Repeats till no more Ca2+ or ATP can not be regenerated

21
Q

ATP regeneration

A

Creatine phosphate
Glucose from glycogen
Aerobic respiration
Anaerobic respiration

22
Q

Anaerobic respiration and death

A

Anaerobic respiration continuous after death till pH fall below 5.4

23
Q

Post-Mortem Changes

A

Low temperature inhibits membrane pump that removes Ca2+
causing contraction as long as ATP is present and pH above 6
When Ca2+ is always present will continue until ATP not join

Once ATP is used muscle becomes locked (Rigor mortis)

Muscle is now shortened, hardened and difficult to chew
If can keep muscle extended then get a tender meat

24
Q

How to extend muscle after death

A

Do not chill while ATP us present
Slow cooling reduce 15-20 degrees for 10 hours
This allows ATP to be used while Ca2+ pump is still active
But it is good conditions for micro-organisms to grow to needs to be good hygiene conditions

25
Q

Lean muscle composition

A

75% water
21% protein
3% fat

26
Q

Bound water and meat

A

Water molecules that are interacting directly with charge side chains on protein

27
Q

Intermediate water and meat

A

Water molecules that are bound to bound water molecules

28
Q

Free water and meat

A

Not interacting with protein or held via surface tension

29
Q

Water in meat and colour

A

Excess free water - wet surface and cut muscle reflects light and looks pale

30
Q

Isoelectric point of Meat

A

approximately 5.2
Amount of bound and intermediate water minimized at this pH and free water maximised

As pH increases or decreases around this point water holding capacity increases

31
Q

Pale, Soft and exudative Meat

PSE

A

Excessive formation of lactic acid
Short term stress - adrenalin causes glycogen to release large amount of water
Caused by rough handling or washing before slaughter

32
Q

Dark, firm and dry Meat

DFD

A
Depletion of glycogen stores before death
So no glucose - pH above 6
Exhaustion
Long transport before slaughter
Prolonged stress
33
Q

Hanging meat

A

Purpose to improve meat quality

Allow endogenous protease in cells to partially degrade muscle sarcomeres and collagen

34
Q

Hanging method

A
Remove intestines and skin
Store for 2 or more weeks
Keep temp at 2-3 degrees - bacteria growth slow but enzymes still active
Control humidity to 85%
No oxygen in meat