Degradation in the rumen of proteins of 2 legumes: soybean meal and field pea
Autor: | Jocelyne Aufrere, Brigitte Michalet-Doreau, Dominique Graviou |
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Přispěvatelé: | Station de recherches sur la nutrition des herbivores, Institut National de la Recherche Agronomique (INRA), ProdInra, Migration, Revues Inra, Import |
Rok vydání: | 1994 |
Předmět: |
Rumen
Nitrogen Soybean meal Protein degradation 03 medical and health sciences Field pea Enzymatic hydrolysis [SDV.BDD] Life Sciences [q-bio]/Development Biology Endopeptidases Animals [SDV.SA.SPA] Life Sciences [q-bio]/Agricultural sciences/Animal production studies Food science Polyacrylamide gel electrophoresis [SDV.BDLR] Life Sciences [q-bio]/Reproductive Biology ComputingMilieux_MISCELLANEOUS Plant Proteins 0303 health sciences Plants Medicinal biology 030306 microbiology Streptomyces griseus 0402 animal and dairy science Proteolytic enzymes food and beverages Fabaceae 04 agricultural and veterinary sciences biology.organism_classification Animal Feed 040201 dairy & animal science [SDV.AEN] Life Sciences [q-bio]/Food and Nutrition Kinetics Biochemistry [SDV.SA.SPA]Life Sciences [q-bio]/Agricultural sciences/Animal production studies Electrophoresis Polyacrylamide Gel Soybeans Digestion |
Zdroj: | Reproduction Nutrition Development Reproduction Nutrition Development, EDP Sciences, 1994, 34, pp.483-490 |
ISSN: | 0926-5287 1297-9708 |
Popis: | Ruminal protein degradation of soybean meal and field pea were compared using 2 analytical methods: in situ and a laboratory analysis with a proteolytic enzyme extracted from Streptomyces griseus. The degradation of total nitrogen in nylon bags of the feeds was measured between 0 and 48 h in the rumen of 2 cows (theoretical degradability: 70.0% for soybean meal and 94.7% for field pea). Electrophoresis of proteins of feeds and in situ residues, in sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) showed that both species have the same type of proteins (7S and 11S) which were degraded in a similar manner in the rumen. The 7S fraction was degraded rapidly whereas the 11S fraction was more resistant. The electrophoretic profiles showed that protein components were less degraded after enzymatic than in situ degradation. In the supernatant after enzymatic hydrolysis, protein and peptides were found in large concentrations and alpha-amino nitrogen and ammonia in low concentrations. It was difficult to simulate the in vitro activity of enzyme complexes in the rumen and the results must be confirmed by direct measurement of the rumen liquid. |
Databáze: | OpenAIRE |
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