The denaturation of whey proteins in a processed cheese environment

被引:0
|
作者
Lee, Siew Kim [1 ,2 ,3 ]
Klostermeyer, Henning [1 ,2 ]
Anema, Skelte G. [1 ,2 ]
机构
[1] Tech Univ Munich, Forschungszentrum Milch & Lebensmittel Weihensteph, D-85354 Freising Weihenstephan, Germany
[2] Tech Univ Munich, Lehrstuhl Chem Biopolymere, D-85350 Freising Weihenstephan, Germany
[3] Fonterra Res & Dev Ctr, Palmerston North, New Zealand
关键词
IRREVERSIBLE THERMAL-DENATURATION; BOVINE BETA-LACTOGLOBULIN; ALPHA-LACTALBUMIN; REACTION-KINETICS; RENNET CASEIN; AGGREGATION; MILK; PH; MELTABILITY; ANALOGS;
D O I
10.1016/j.idairyj.2024.105897
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The kinetics of whey protein denaturation at three pH values (pH 5.4, 5.7 and 6.0) was determined in processed cheese made from rennet casein/whey protein concentrate (RC -PC), or milk protein concentrate (MPC-PC). Samples were heated from 75 to 100 degrees C for up to 5400 s. Denaturation of both proteins was faster with increasing pH. The reaction order for b-lactoglobulin and a-lactalbumin denaturation was 1.5 and 1.0 respectively. There was a change in temperature dependence of the rate constants at about 85 degrees C for both proteins. Kinetic parameters were consistent with unfolding as rate-determining at low temperatures and aggregation as rate-determining at higher temperatures. b-Lactoglobulin denaturation was slower at low temperatures and faster at high temperatures for the MPC-PC when compared with RC -PC with a similar effect at all pH. a-Lactalbumin denaturation was more rapid for MPC-PC than RC -PC at all temperatures, with a greater difference at lower pH. (c) 2024 Elsevier Ltd. All rights reserved.
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页数:11
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