Textural properties of cold-set gels induced from heat-denatured whey protein isolates

Z. Y. Ju, A. Kilara

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

Abstract

A 9% whey protein (WP) isolate solution at pH 7.0 was heat-denatured at 80°C 30 min. Size-exclusion HPLC showed that native WP formed soluble aggregates after heat-treatment. Additions of CaCl2 (10-40 nM), 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.

Original languageEnglish (US)
Pages (from-to)288-292
Number of pages5
JournalJournal of Food Science
Volume63
Issue number2
DOIs
StatePublished - Jan 1 1998

All Science Journal Classification (ASJC) codes

  • Food Science

Fingerprint Dive into the research topics of 'Textural properties of cold-set gels induced from heat-denatured whey protein isolates'. Together they form a unique fingerprint.

Cite this