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
Original language | English |
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Pages (from-to) | 2229-2238 |
Journal | Journal of the Science of Food and Agriculture |
Volume | 87 |
Issue number | 12 |
DOIs | |
Publication status | Published - 2007 |
Keywords
- n-15-isotope dilution technique
- small-intestinal mucus
- beta-lactoglobulin
- enzymatic extractability
- soy proteins
- growing pigs
- glycine-max
- hydrolysis
- proteolysis
- glycoprotein