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dc.contributor.author
Colombatto, Dario
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dc.contributor.author
Beauchemin, K. A.
dc.date.available
2020-08-28T18:06:46Z
dc.date.issued
2009-03
dc.identifier.citation
Colombatto, Dario; Beauchemin, K. A.; A protease additive increases fermentation of alfalfa diets by mixed ruminal microorganisms in vitro; American Society of Animal Science; Journal of Animal Science; 87; 3; 3-2009; 1097-1105
dc.identifier.issn
0021-8812
dc.identifier.uri
http://hdl.handle.net/11336/112666
dc.description.abstract
In vitro experiments were conducted to examine the characteristics and mode of action of a protease that increased the ruminai fiber digestibility of alfalfa hay. A commercial source of protease (Protex 6L, Genencor Int., Rochester, NY), already characterized for its main activities, was further analyzed to determine protease activity in response to pH, molecular size by SDS-PAGE, specificity to degrade model or feed substrates, response to autoclaving, and action of specific protease inhibitors in the absence or presence of ruminai fluid. In addition, batch culture in vitro incubations in buffered ruminal fluid were conducted to compare the enzyme product with purified protease sources, and dose-response studies (0 to 10 μL/g of forage DM) were carried out using alfalfa hay as a substrate. The enzyme product was shown to be an alkaline protease (optimum pH >8.5) of approximately 30 kDa. Specificity in the absence of ruminai fluid showed that the enzyme was active against gelatin and casein to the same extent, whereas it had limited (21% of the total) activity on BSA. In the presence of ruminai fluid and with the use of feed substrates, the protease increased (P < 0.05) 22-h IVDMD (%) of alfalfa hay, fresh corn silage, dry-rolled corn, and a total mixed ration composed of the 3 ingredients (39.5 vs. 44.7; 50.3 vs. 54.5; 63.8 vs. 68.4; and 55.4 vs. 56.4 for control vs. protease for each feed, respectively). Inhibitor studies in the absence of ruminai fluid indicated that the enzyme was inhibited most by a serine protease inhibitor but not by cysteineor metalloprotease inhibitors (10 vs. 1.9 and 0.1%, respectively). In the presence of ruminal fluid, the serine protease inhibitor reversed (P < 0.05) the increase in alfalfa IVDMD achieved by the enzyme product, such that IVDMD was similar to that of the control treatment. Comparisons among different proteases revealed that only pure subtilisin achieved increases in IVDMD that were similar to those with protease, suggesting the serine protease was subtilisin-like (EC 3.4.1.62). Dose-response studies using alfalfa hay as substraje showed quadratic responses in IVDMD, NDF digestion, and hemicellulose and protein disappearance. It is postulated that this enzyme acts by removing structural proteins in the cell wall, allowing ruminal microbes to gain faster access to digestible substrates.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society of Animal Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
EXOGENOUS PROTEASE
dc.subject
FIBER
dc.subject
IN VITRO DISAPPEARANCE
dc.subject
RUMEN DIGESTIBILITY
dc.subject.classification
Ciencias Veterinarias
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dc.subject.classification
Ciencias Veterinarias
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dc.subject.classification
CIENCIAS AGRÍCOLAS
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dc.title
A protease additive increases fermentation of alfalfa diets by mixed ruminal microorganisms in vitro
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-07-01T17:34:42Z
dc.journal.volume
87
dc.journal.number
3
dc.journal.pagination
1097-1105
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Urbana
dc.description.fil
Fil: Colombatto, Dario. Universidad de Buenos Aires. Facultad de Agronomía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina
dc.description.fil
Fil: Beauchemin, K. A.. Agriculture Et Agroalimentaire Canada; Canadá
dc.journal.title
Journal of Animal Science
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.2527/jas.2008-1262
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jas/article-abstract/87/3/1097/4731175
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