Functional properties of Milk Flashcards
4 physical and chemical changes
coagulation
aeration
foaming
gelation
what happens during cold storage
beta casein dissociates from micelles into milk serum
what associations occur during heat treatment of milk
Conjugation
alpha-lactalbumin and beta-lactoglobulin
K-casein and beta lactoglobulin
what happens to caseins when heat is applied
aggregate and Ca phosphate precipitate releasing H+ making it more acidic
associations between micelles and whey proteins during the heat are caused by
disulphide bridges
hydrogen bonding
hydrophobic interactions
calcium linkages
why arent caseins denatured by heat
their disordered secondary structure
what happens to caseins above boiling temperatures
irreversible aggregation
Ca phosphate precipitates
CO2 is expelled
pH is lowered
buffering capacity decreases
what temperature are whey proteins denatured
60C
four steps to heat-induced whey gelation
unfolding
aggregation
string formation
linkages
what do the structure and consistency of whey proteins depend on
pH
protein formulation/concentration
temp/degree of denaturation
which protein is the most amphiphilic protein in milk
beta casein
why are milk proteins good at emulsifying and foaming
the amphipathic ability of the proteins the hydrophobic is in the fat/air and hydrophillic in the milk solution
methods to improve functional properties
enzymatic modification
chemical modification
physical treatment
types of enzymatic modifications
cross-linking
amino-acid modification
hydrolysis
types of chemical modifications
addition of acid or base
addition of salt
conjugation to other biochemical molecules (fatty acids)