In situ rumen degradation of amino acids from different feeds corrected for microbial contamination

[EN]: Variations of the amino acid profile produced by rumen actions were established for fish meal (FM), corn grain (CG), corn gluten feed (GF), dehydrated beet pulp (DBP), and lucerne hay (LH), using the nylon bag technique. The effects of degradation of soluble or insoluble proteins were measured...

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Detalles Bibliográficos
Autores: González, Javier, Centeno, Carmen, Lamrani, Farida, Rodríguez, Carlos Alberto
Tipo de recurso: artículo
Fecha de publicación:2001
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/257110
Acceso en línea:http://hdl.handle.net/10261/257110
Access Level:acceso abierto
Palabra clave:Rumen degradation
Microbial contamination
Amino acid profile
Contamination microbienne
Dégradation ruminale
Profil des acides aminés
15N
Descripción
Sumario:[EN]: Variations of the amino acid profile produced by rumen actions were established for fish meal (FM), corn grain (CG), corn gluten feed (GF), dehydrated beet pulp (DBP), and lucerne hay (LH), using the nylon bag technique. The effects of degradation of soluble or insoluble proteins were measured by rumen incubations at 0 h (washout value) and 16 h, respectively. Rumen incubations were performed on four cannulated wethers and the microbial contamination of incubated residues was corrected using a continuous 15N-intraruminal infusion and solid associated bacteria isolates as the reference sample. The results showed that rumen degradation of both soluble and insoluble proteins produced changes in the amino acid profile, which were not uniform among feeds. Differences between feed and insoluble protein amino acid composition were limited for FM and DBP, important for GF and LH, and intermediate for CG. Differences between insoluble and undegraded protein amino acid composition were also limited for FM, GF, DBP, and LH and important in CG. The results showed that the amino acid profile in the undegraded protein and in the whole feed should be close for FM, DBP and LH. On the contrary, in CG, important variations are expected, since both solubility and degradability effects produced changes with the same tendency for most of the essential amino acids. In particular, our results showed a great decrease in the lysine content of the undegraded protein, which increases the lysine deficiency of this feed. This decrease of lysine was also evidenced in GF.