Production, purification, and characterization of a highly glucose-tolerant novel beta-glucosidase from Candida peltata
نویسندگان
چکیده
منابع مشابه
Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae.
Aspergillus oryzae was found to secrete two distinct beta-glucosidases when it was grown in liquid culture on various substrates. The major form had a molecular mass of 130 kDa and was highly inhibited by glucose. The minor form, which was induced most effectively on quercetin (3,3',4',5,7-pentahydroxyflavone)-rich medium, represented no more than 18% of total beta-glucosidase activity but exhi...
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Jian Lu1, Liqin Du1, Yutuo Wei1, Yuanyuan Hu1, and Ribo Huang1,2* State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, College of Life Science and Technology, Guangxi University, Nanning 530005, China National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, Nanning 530004, China These authors contributed equally to this work....
متن کاملExpression and characterization of a novel highly glucose-tolerant β-glucosidase from a soil metagenome.
A β-glucosidase gene unbgl1A was isolated by the function-based screening of a metagenomic library and the enzyme protein was expressed in Escherichia coli, purified, and biochemically characterized. The enzyme Unbgl1A had a Km value of 2.09 ± 0.31 mM, and a Vmax value of 183.90 ± 9.61 μmol min(-1) mg(-1) under the optimal reaction conditions, which were pH 6.0 at 50°C. Unbgl1A can be activated...
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β-Glucosidase is an important component of the cellulase complex. It not only hydrolyzes cellobiose and short-chain cellooligosaccharides to glucose, but also removes the inhibitory effect of cellobiose on the β-1, 4-endoglucanase and exoglucanase, thereby increasing the overall rate of cellulose biodegradation. β-glucosidasefrom culture supernatant of a fungus Penicillium simplicissimum was pu...
متن کاملPurification, characterization, gene cloning, and sequencing of a new beta-glucosidase from Bacillus circulans subsp. alkalophilus.
An intracellular beta-glucosidase was purified from cell extracts of Bacillus circulans subsp. alkalophilus by NAD affinity and high-performance anion-exchange chromatographies. The enzyme was active against a wide range of aryl-beta-glucosides and beta-linked disaccharides. The structural gene for beta-glucosidase was cloned in Escherichia coli. The beta-glucosidase gene consisted of an open r...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1996
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.62.9.3165-3170.1996