Degradation in the rumen of proteins of 2 legumes: soybean meal and field pea

Autor: Jocelyne Aufrere, Brigitte Michalet-Doreau, Dominique Graviou
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