Bioprospecting metagenomes: glycosyl hydrolases for converting biomass
نویسندگان
چکیده
منابع مشابه
Bioprospecting metagenomes: glycosyl hydrolases for converting biomass
Throughout immeasurable time, microorganisms evolved and accumulated remarkable physiological and functional heterogeneity, and now constitute the major reserve for genetic diversity on earth. Using metagenomics, namely genetic material recovered directly from environmental samples, this biogenetic diversification can be accessed without the need to cultivate cells. Accordingly, microbial commu...
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BACKGROUND To efficiently deconstruct recalcitrant plant biomass to fermentable sugars in industrial processes, biocatalysts of higher performance and lower cost are required. The genetic diversity found in the metagenomes of natural microbial biomass decay communities may harbor such enzymes. Our goal was to discover and characterize new glycoside hydrolases (GHases) from microbial biomass dec...
متن کاملNomenclature for sugar-binding subsites in glycosyl hydrolases.
The huge structural diversity of polysaccharides leads to their central roles in food storage and utilization, structure, cell–cell signalling, cell-wall expansion and turnover and viral invasion. Glycosyl hydrolases, enzymes hydrolysing the glycosidic bond in di-, oligoand poly-saccharides, are found in all living organisms. The first X-ray structural determination of an enzyme was of a glycos...
متن کاملETHANOL PRECIPITATION OF GLYCOSYL HYDROLASES PRODUCED BY Trichoderma harzianum P49P11
This study aimed to concentrate glycosyl hydrolases produced by Trichoderma harzianum P49P11 by ethanol precipitation. The variables tested besides ethanol concentration were temperature and pH. The precipitation with 90% (v/v) ethanol at pH 5.0 recovered more than 98% of the xylanase activity, regardless of the temperature (5.0, 15.0, or 25.0 °C). The maximum recovery of cellulase activity as ...
متن کاملDetermination of the catalytic base in family 48 glycosyl hydrolases.
The catalytic base in family 48 glycosyl hydrolases has not been previously established experimentally. Based on structural and modeling data published to date, we used site-directed mutagenesis and azide rescue activity assays to show definitively that the catalytic base in Thermobifida fusca Cel48A is aspartic acid 225. Of the tested mutants, only Cel48A with the D225E mutation retained parti...
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ژورنال
عنوان ژورنال: Biotechnology for Biofuels
سال: 2009
ISSN: 1754-6834
DOI: 10.1186/1754-6834-2-10