Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 369500
Title Presence of indigestible peptide aggregates of soybean meal in pig ileal digesta residue
Author(s) Fischer, M.; Voragen, A.G.J.; Piersma, S.R.; Kofod, L.V.; Joergensen, C.I.; Guggenbuhl, P.; Nunes, C.S.; Gruppen, H.
Source Journal of the Science of Food and Agriculture 87 (2007)12. - ISSN 0022-5142 - p. 2229 - 2238.
DOI https://doi.org/10.1002/jsfa.2948
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) n-15-isotope dilution technique - small-intestinal mucus - beta-lactoglobulin - enzymatic extractability - soy proteins - growing pigs - glycine-max - hydrolysis - proteolysis - glycoprotein
Abstract With the purpose of analysing the molecular size and composition, proteinaceous material was extracted from the insoluble components of a digesta sample obtained from pigs fed a feed consisting of only soybean meal. Gel permeation chromatography indicated that the alkali-extractable fraction of the proteinaceous material from the residue was of relatively high apparent molecular weight. However, the combined results from gel electrophoresis, RPLC-MS, and MALDI-ToF MS showed that the extracted protein material was in fact, to a high extent, composed of aggregated peptides. To our knowledge this has not previously been described. Aggregates extracted by dilute alkali were fully degraded upon subsequent proteolytic treatment. N-terminal sequencing of selected protein bands from SDS-PAGE gels indicated the presence of partly degraded -conglycinin alpha subunits in the residue
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