Aggregation of peptides during hydrolysis as a cause of reduced enzymatic extractability of soybean meal proteins

M. Fischer, H. Gruppen, S.R. Piersma, L.V. Kofod, H.A. Schols, A.G.J. Voragen

Research output: Contribution to journalArticleAcademicpeer-review

24 Citations (Scopus)

Abstract

With the purpose of analyzing the size and composition of enzyme-unextractable proteins in differently heat-treated soybean meals, a selection of extractants was screened for their ability to extract these proteins from enzyme-unextractable residues. The largest effects were obtained with urea, urea plus -mercaptoethanol, and dilute alkali; the latter extracted up to 87␘f the enzyme-unextractable protein. Gel permeation chromatography indicated that a large proportion of the extracted material was of high molecular weight. However, the combined results from gel electrophoresis, LC-MS, and MALDI-ToF MS showed that the extracted protein material was composed of aggregated peptides. The largest aggregates were observed in the enzymatic residues originating from meals heat-treated at high humidity. Extracted aggregates were fully degraded upon subsequent proteolytic treatment
Original languageEnglish
Pages (from-to)4512-4519
JournalJournal of Agricultural and Food Chemistry
Volume50
DOIs
Publication statusPublished - 2002

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