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Textural Properties of Cold‐set Gels Induced from Heat‐denatured Whey Protein Isolates
Author(s) -
JU Z. Y.,
KILARA A.
Publication year - 1998
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.1365-2621.1998.tb15728.x
Subject(s) - chemistry , bacillus licheniformis , hydrolysis , whey protein , salt (chemistry) , protease , chromatography , sodium , whey protein isolate , enzyme , bacteria , biochemistry , organic chemistry , bacillus subtilis , genetics , biology
A 9% whey protein (WP) isolate solution at pH 7.0 was heat‐denatured at 80°C for 30 min. Size‐exclusion HPLC showed that native WP formed soluble aggregates after heat‐treatment. Additions of CaCl2 (10–40 mM), NaCl (50–400 mM) or glucono‐delta‐lactone (GDL, 0.4–2.0%, w/v) or hydrolysis by a protease from Bacillus licheniformis caused gelation of the denatured solution at 45°C. Textural parameters, hardness, adhesiveness, and cohesiveness of the gels so formed changed markedly with concentration of added salts or pH by added GDL. Maximum gel hardness occurred at 200 mM NaCl or pH 4.7. Increasing CaCl2 concentration continuously increased gel hardness. Generally, GDL‐induced gels were harder than salt‐induced gels, and much harder than the protease‐induced gel.