Presence of indigestible peptide aggregates of soybean meal in pig ileal digesta residue
| Autor: | Christian Isak Joergensen, Lene Venke Kofod, Morten Fischer, Harry Gruppen, Alphons G. J. Voragen, Carlos Simões Nunes, P. Guggenbuhl, Sander R. Piersma |
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| Rok vydání: | 2007 |
| Předmět: |
glycoprotein
proteolysis Soybean meal Peptide Gel permeation chromatography Residue (chemistry) Hydrolysis glycine-max Enzymatic hydrolysis Levensmiddelenchemie Beta-lactoglobulin VLAG Gel electrophoresis chemistry.chemical_classification Nutrition and Dietetics Chromatography Food Chemistry beta-lactoglobulin biology Chemistry small-intestinal mucus n-15-isotope dilution technique soy proteins growing pigs enzymatic extractability hydrolysis biology.protein Agronomy and Crop Science Food Science Biotechnology |
| Zdroj: | Journal of the Science of Food and Agriculture, 87(12), 2229-2238 Journal of the Science of Food and Agriculture 87 (2007) 12 |
| ISSN: | 1097-0010 0022-5142 |
| DOI: | 10.1002/jsfa.2948 |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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