Isolation and characterization of a novel glycosyl hydrolase family 74 (GH74) cellulase from the black goat rumen metagenomic library
Language English Country United States Media print-electronic
Document type Journal Article
PubMed
27866354
DOI
10.1007/s12223-016-0486-3
PII: 10.1007/s12223-016-0486-3
Knihovny.cz E-resources
- MeSH
- Rumen microbiology MeSH
- Cellulase chemistry genetics isolation & purification MeSH
- Escherichia coli genetics metabolism MeSH
- Gene Expression MeSH
- Fibrobacter enzymology genetics MeSH
- Genetic Testing MeSH
- Gene Library MeSH
- Cloning, Molecular MeSH
- Hydrogen-Ion Concentration MeSH
- Goats microbiology MeSH
- Metagenome * MeSH
- Metagenomics MeSH
- Molecular Weight MeSH
- Recombinant Proteins genetics isolation & purification metabolism MeSH
- Sequence Homology MeSH
- Enzyme Stability MeSH
- Substrate Specificity MeSH
- Temperature MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Cellulase MeSH
- Recombinant Proteins MeSH
This study aimed to isolate and characterize a novel cellulolytic enzyme from black goat rumen by using a culture-independent approach. A metagenomic fosmid library was constructed from black goat rumen contents and screened for a novel cellulase. The KG37 gene encoding a protein of 858 amino acid residues (92.7 kDa) was isolated. The deduced protein contained a glycosyl hydrolase family 74 (GH74) domain and showed 77% sequence identity to two endo-1,4-β-glucanases from Fibrobacter succinogenes. The novel GH74 cellulase gene was overexpressed in Escherichia coli, and its protein product was functionally characterized. The recombinant GH74 cellulase showed a broad substrate spectrum. The enzyme exhibited its optimum activity at pH 5.0 and temperature range of 20-50 °C. The enzyme was thermally stable at pH 5.0 and at a temperature of 20-40 °C. The novel GH74 cellulase can be practically exploited to convert lignocellulosic biomass to value-added products in various industrial applications in future.
Department of Biological Sciences Kyonggi University Suwon 442 760 South Korea
Department of Food Science and Technology Chung Ang University Ansung 456 756 South Korea
See more in PubMed
Appl Environ Microbiol. 2002 Apr;68(4):1556-60 PubMed
J Basic Microbiol. 2008 Dec;48(6):464-72 PubMed
Nucleic Acids Res. 2012 Jan;40(Database issue):D290-301 PubMed
Biochem Biophys Res Commun. 2013 Nov 22;441(3):567-72 PubMed
Biosci Biotechnol Biochem. 2012;76(6):1075-84 PubMed
J Biol Chem. 1996 Aug 30;271(35):21268-72 PubMed
J Dairy Sci. 1997 Jan;80(1):167-75 PubMed
Appl Environ Microbiol. 2005 Dec;71(12):7670-8 PubMed
Enzyme Res. 2011;2011:280696 PubMed
Chem Biol. 1998 Oct;5(10):R245-9 PubMed
Appl Microbiol Biotechnol. 2007 May;75(2):319-28 PubMed
Anim Biotechnol. 2012;23(4):261-77 PubMed
Appl Environ Microbiol. 1982 Apr;43(4):777-80 PubMed
Biotechnol Adv. 1997;15(3-4):583-620 PubMed
FEBS Lett. 2002 Nov 6;531(2):375-80 PubMed
Eur J Biochem. 2003 Jul;270(14):3083-91 PubMed
FEMS Microbiol Rev. 2003 Dec;27(5):663-93 PubMed
Appl Environ Microbiol. 1996 Feb;62(2):316-22 PubMed
Nucleic Acids Res. 2010 Jul;38(12):e132 PubMed
BMC Res Notes. 2012 Oct 13;5:566 PubMed
Cellulolytic thermophilic microorganisms in white biotechnology: a review