Linked Life Data

20890102

Source:http://linkedlifedata.com/resource/pubmed/id/20890102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2010-10-4
pubmed:databankReference
pubmed:abstractText
The demand for beta-glucosidases insensitive to product inhibition is increasing in modern biotechnology, for these enzymes would improve the process of saccharification of lignocellulosic materials. In this study, a beta-glucosidase gene which encodes a 442-amino-acid protein was isolated from a marine microbial metagenomic library by functional screening and named as bgl1A. The protein was identified to be a member of GH1 family, and was recombinantly expressed, purified and biochemically characterized. The recombinant beta-glucosidase, Bgl1A, exhibited high level of stability in the presence of various cations and high concentrations of NaCl. Interestingly, it was activated by glucose at concentrations lower than 400 mM. With glucose further increasing, the enzyme activity of Bgl1A was gradually inhibited, but remained 50% original value in even as high as 1,000 mM glucose. These findings indicate Bgl1A might be a potent candidate for industrial applications.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1017-7825
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1351-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Cloning and characterization of a beta-glucosidase from marine microbial metagenome with excellent glucose tolerance.
pubmed:affiliation
School of Life Sciences and Biotechnology Center, Anhui University, Hefei, Anhui, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't