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J Agric Food Chem. 2002 Jul 31;50(16):4512-9.

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

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  • 1Centre for Protein Technology TNO-WU, P.O. Box 8129, 6700 EV Wageningen, The Netherlands.


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 beta-mercaptoethanol, and dilute alkali; the latter extracted up to 87% of 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.

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