Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate

W. A.M. Mutilangi, D. Panyam, A. Kilara

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179 Scopus citations

Abstract

Heat-denatured whey protein isolate was hydrolyzed with trypsin, α-chymotrypsin, Alcalase or Neutrase to 2.8, 4.3, 6.0 or 8.0% degree of hydrolysis. Hydrolysates were fractionated by ultrafiltration and freezedried. Protein content of retentates showed little variation but permeates differed with enzyme. Surface hydrophobicity increased with hydrolysis but was not linear except for α-chymotrypsin. Ultrafiltration increased solubility and the permeates and retentates had better solubility than hydrolysates. Retentates had higher emulsifying activity index than hydrolysates while permeates did not form stable emulsions. Permeates formed stable foams but hydrolysates and retentates showed poor foaming characteristics. Specificity of the enzyme, and degree of hydrolysis influenced the functional properties of the peptides. Fractions generated by trypsin, at all levels of hydrolysis generally had higher solubility, emulsifying properties and foaming properties. Permeates from Alcalase hydrolysis had the best foam capacity but low foam stability.

Original languageEnglish (US)
Pages (from-to)270-275
Number of pages6
JournalJournal of Food Science
Volume61
Issue number2
StatePublished - Jan 1 1996

All Science Journal Classification (ASJC) codes

  • Food Science

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