Soluble in weak
salt solutions:
myosin (muscle
tissue),
lactoglobins (milk)
Soluble in acids:
wheat glutenin,
oryzenin (rice)
Water bindning
Through
hydrogen
bonding w/-
muscle tissue
of meats
(ground
products ie hot
dogs, mince)
Structure
Primary: molecular weight, aa
composition & seq along
peptide chain.
Secondary: shape of coiled helix
Tertiary: folding of a chain over itself
quartenary: 2 or
more polypeptide
chains join
Changed through
food processing
Denaturation: change in
strcuture without
breaking covalent
bonds, or aa seq.
Loss of biological activity & changes
in physical/functional proeprties (ie
solubility)
Caused by heat, acids, solvents,
concetrated salts, surface forces.
eg. 'Blanching; in freezing/canning
fruits & veg, Cheeses/Yogurts,
Hardening of egg whit in pan (heat
denaturation), whipping of egg
whites to foam (surface force), slow
cooking meat.
Contributes to
flavour & texture
of food.
Reduction:
Hydrolysis: cleaving of peptide bonds
by adding water molecule.
Complete: P broken down to aa cparts
Partial: protein hydrolsates,: flavours parts of soups, sauces, gravy. plant
prteins hydrolysed by hydrochloric acid - neuatralised with alkali.