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Empirical Observations and Thermodynamical Considerations on Water‐Binding by Whey Proteins in Food Products
Author(s) -
WIT J. N.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb09322.x
Subject(s) - sterilization (economics) , whey protein , chemistry , food science , gelatin , lactalbumin , biochemistry , monetary economics , economics , foreign exchange market , foreign exchange
Basic protein knowledge is used to explain protein functionality in food products. Empirical observations on the water‐binding capacity of whey protein concentrate and gelatin during cooling in set yoghurt and during sterilization of meat products are discussed in terms of effects of temperature on the structure and thermodynamic behavior of their main protein isolates: α‐Lactalbumin and tropocollagen, respectively. It appears that the water‐binding of proteins is governed by their thermally induced folding behavior. In particular, the greater tendency of whey proteins to fold at low temperature due to hydrophobic effects, and to remain dispersed at high temperatures as a result of disorder effects, keeps these proteins from water‐retention in a network structure during cooling and sterilization.