Isolation and characterization of a novel endo-beta-1, 4-glucanase from a metagenomic library of the black-goat rumen
Braz. j. microbiol
;
48(4): 801-808, Oct.-Dec. 2017. tab, graf
Artículo
en Inglés
| LILACS
| ID: biblio-889172
ABSTRACT
ABSTRACT The various types of lignocellulosic biomass found in plants comprise the most abundant renewable bioresources on Earth. In this study, the ruminal microbial ecosystem of black goats was explored because of their strong ability to digest lignocellulosic forage. A metagenomic fosmid library containing 115,200 clones was prepared from the black-goat rumen and screened for a novel cellulolytic enzyme. The KG35 gene, containing a novel glycosyl hydrolase family 5 cellulase domain, was isolated and functionally characterized. The novel glycosyl hydrolase family 5 cellulase gene is composed of a 963-bp open reading frame encoding a protein of 320 amino acid residues (35.1 kDa). The deduced amino acid sequence showed the highest sequence identity (58%) for sequences from the glycosyl hydrolase family 5 cellulases. The novel glycosyl hydrolase family 5 cellulase gene was overexpressed in Escherichia coli. Substrate specificity analysis revealed that this recombinant glycosyl hydrolase family 5 cellulase functions as an endo-β-1,4-glucanase. The recombinant KG35 endo-β-1,4-glucanase showed optimal activity within the range of 30-50 °C at a pH of 6-7. The thermostability was retained and the pH was stable in the range of 30-50 °C at a pH of 5-7.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Rumen
/
Bacterias
/
Proteínas Bacterianas
/
Celulasa
Límite:
Animales
Idioma:
Inglés
Revista:
Braz. j. microbiol
Asunto de la revista:
Microbiologia
Año:
2017
Tipo del documento:
Artículo
País de afiliación:
Corea del Sur
Institución/País de afiliación:
Chung-Ang University/KR
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