Food Chem Flashcards
(25 cards)
Amino acid
A alpha carbon which has a carboxyl group and a amino group
Peptide
Amino acids which has undergone condensation. Condensation creates peptide link thus now a peptide.
Protien
A chain of amino acids consisting of 50 or more amino acids, each joined by peptide links
Primary structure
A sequence of amino acids
Secondary structure
Alpha helixes and beta pleated sheets, derived from hydrogen bonding between N-H and C=O group. Slightly positive H in N-H hydrogen bonds with slightly negative O in C=O
Tertiary structure
Overall 3D structure of the protein is derived from intermolecular interactions between groups in amino acid side chains. Looks at how the alpha helixes and beta pleated plates interact. Dispersion forces, Hydrogen bonds, dipole bonds, ionic interactions and disulphide bridge in cys-cys
Quaternary structure
How protein with other proteins in 3D
Rancidity of fats + antioxident
Two stages:
Initiation: C=C oxidizes and forms a free radical
Propagation: chain reaction (auto-oxidation) forming harmful short chains containing aldehyde and keytones, the smell is from aldehyde
An antioxidant oxidizes in preference to the C=C thus, preventing/delaying rancidity of fat or donating H+ to prevent oxidation
To prevent rancidity:
-lower temperature thus lower rate of reaction
-use lean meats, avoid fat
-use saturated fats
Glycemic index
The rate of release of glucose into the bloodstream within two hours. Pure glucose has a relative GI of 100.
Starch (carbohydrate)
Amylose: Straight thus more dispersion forces hence harder to break down by amylase into maltose. Low GI
Amylopectin: Branches thus fewer dispersion forces hence easier to breakdown by amylase into maltose. High GI
Made of alpha glucose
Glycogen
Extremely branched, used for energy storage. Since it is so branched it can be easily broken down into glucose. Made due to excess glucose
Made of alpha glucose
Celluose
Not branched thus very strong bonds. Humans cannot ingest cellulose due to lack in cellulase.
Celluose made from Beta glucose
Maltose
A disaccharide that is made from two alpha glucose
Sucrose
A disaccharide that is made from glucose and fructose
Lactose
A disaccharide that is made from galactose and glucose
Glucose
Alpha glucose has OH on the first C facing down
Beta glucose has OH on the first C facing up
Fructose
Pentagonal structure
Galactose
fourth C’s OH is facing up compared to glucose
Vitamin
Polar
-More OH groups
-Dissolved in blood
-Blood pass through the liver and thus is excreted
-lots needed
-C and B
Non-Polar
-Little OH groups
-Stored in fatty tissue
-Not needed in large quantities because fat is not easily ridden
Digestion of carbohydrates
Amylose and amylopectin are broken down into maltose by amylase in salvia. Crushing the food increases surface area thus higher rate of reaction
Maltose is broken down into glucose by maltase in the small intestine
Digestion of protiens
Proteins or polypeptides, start digestion in the stomach. Pepsin breaks it down into dipeptides
Dipeptides are broken down into amino acids for the body to absorb by proteas in small intestine
Digestion of triglycerides
Triglyceride is broken down by lipase in the small intestine.
In the small intestine, bile drips down from the pancreas, emulsifying the fat globule
Smaller fat droplets form as a result as bile surrounds it thus it increases in surface area
Lipase enters the small intestine from the pancreas catalyzing the hydrolysis process of fat droplets
Lipase is polar and thus can only interact with the surface of the nonpolar fat droplet however due to droplet size it can react with the whole thing
Enzyme + Co enzymes
Enzymes:
- catalyze reaction thus rate of reaction increase and not equilibrium point
- lock and key model predicts that enzyme has specific shape for specific substrate
- induced fit model predicts that enzyme can slightly alter shape by the binding of the substrate however it is still highly specific and can normally only change shapes for isomer of substrate
-Does not change as a result of reaction
Co enzymes
- acts as a proton donor or small molecule donor
- helps substrate physically fit into enzyme as coenzyme changes the tertiary structure of enzyme protein
-can change as a result of the reaction
Denaturisation of enyzme
Enzyme is denaturized through extreme pHs or temperatures
Secondary and tertiary structures are broken as a result of breaking the intermolecular bonds
At low pH, the COO group will not ionise thus it will not be negatively charged
AT high pH, the NH3 will not act as base thus it will not be charged
High temperatures literally break the tertiary structure of protein however primary structure is not affected as it is the peptide links.
High temperatures cause the unfolding of the protein chain/s thus causing them to clump together afterward. This known as coagulation