Resultados de búsqueda - Ruiz, B
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ACTIVACIÓN QUÍMICA DE OVOCITOS DE ALPACA VITRIFICADOS DESPUÉS DE LA MADURACIÓN IN VITRO
Publicado 2011Fuente: RedalycTipo de material: Artículo científicoAcceso al recurso -
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Florfenicol concentrations in milk of lactating cows postreated by intramuscular or intramammary routes
Publicado 2010Fuente: RedalycTipo de material: Artículo científicoAcceso al recurso -
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Evaluación de los efectos de dos protocolos anestésicos aplicados durante ovariohisterectomía sobre hemograma, creatinina, BUN, ALT y FA en hembras caninas
Publicado 2010Fuente: RedalycTipo de material: Artículo científicoAcceso al recurso -
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Medición de las enzimas AST y GGT en diferentes estados reproductivos y/o edades en caballo Criollo Colombiano en el Valle de Aburrá, Antioquia
Publicado 2010Fuente: RedalycTipo de material: Artículo científicoAcceso al recurso -
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Evaluación del efecto de la alimentación y de la administración de omeprazol en pellets vía oral sobre el pH del jugo gástrico en equinos adultos
Publicado 2012Fuente: RedalycTipo de material: Artículo científicoAcceso al recurso -
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Draft Genome Sequence of Bacillus amyloliquefaciens JJC33M, Isolated from Sugarcane Soils in the Papaloapan Region, Mexico
Publicado 2015Fuente: Universidad del PapaloapanTipo de material: ArtículoDescripción: Bacillus amyloliquefaciens strain JJC33M is a bacterium that produces α-amylase (EC 3.2.1.1) and was isolated from sugarcane soil. Its estimated genome size is 3.96 Mb, and it harbors 4,048 coding genes (CDSs).Acceso al recurso -
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Effect of differential processing of the native and recombinant α-amylase from Bacillus amyloliquefaciens JJC33M on specificity and enzyme properties
Publicado 2017Fuente: Universidad del PapaloapanTipo de material: ArtículoDescripción: AmyJ33, an α-amylase isolated from Bacillus amyloliquefaciens JJC33M, has been characterized as a non-metalloenzyme that hydrolyzes raw starch. In this work, the gene that codifies for AmyJ33 was isolated and cloned. The recombinant α-amylase (AmyJ33r) produced had a molecular weight of 72 kDa, 25 kDa higher than the native α-amylase (AmyJ33). Our results suggest that the C-terminal was processed in a different way in the native and the recombinant enzyme causing the difference observed in the molecular weight. Additionally, the enzyme activity, specificity and biochemical behavior were affected by this larger C-terminal extra region in AmyJ33r, since the enzyme lost the ability to hydrolyze raw starch compared to the native but increased its thermal stability and pH stability, and modified the profile of activity toward alkaline pH. It is suggested that the catalytic domain in recombinant enzyme, AmyJ33r, could be interfered or blocked by the amino acids involved in the C-terminal additional region producing changes in the enzyme properties.Acceso al recurso