Affordable Access

deepdyve-link
Publisher Website

Isolation and characterization of a novel endo-β-1,4-glucanase from a metagenomic library of the black-goat rumen.

Authors
  • Song, Yun-Hee1
  • Lee, Kyung-Tai2
  • Baek, Jin-Young1
  • Kim, Min-Ju1
  • Kwon, Mi-Ra2
  • Kim, Young-Joo2
  • Park, Mi-Rim2
  • Ko, Haesu2
  • Lee, Jin-Sung3
  • Kim, Keun-Sung4
  • 1 Department of Food Science and Technology, Chung-Ang University, Ansung 456-756, South Korea. , (North Korea)
  • 2 Animal Genomics and Bioinformatics Division, National Institute of Animal Science, Rural Development Administration, Wanju, South Korea. , (North Korea)
  • 3 Department of Biological Sciences, Kyonggi University, Suwon, South Korea. Electronic address: [email protected] , (North Korea)
  • 4 Department of Food Science and Technology, Chung-Ang University, Ansung 456-756, South Korea. Electronic address: [email protected] , (North Korea)
Type
Published Article
Journal
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
Publication Date
Jan 01, 2017
Volume
48
Issue
4
Pages
801–808
Identifiers
DOI: 10.1016/j.bjm.2017.03.006
PMID: 28689814
Source
Medline
Keywords
License
Unknown

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 (35.1kDa). 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.

Report this publication

Statistics

Seen <100 times