Characterization of a Salt-Tolerant and Cold-Adapted Xylanase from Bacillus cellulosilyticus
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منابع مشابه
A novel cold-adapted and highly salt-tolerant esterase from Alkalibacterium sp. SL3 from the sediment of a soda lake
A novel esterase gene (estSL3) was cloned from the Alkalibacterium sp. SL3, which was isolated from the sediment of soda lake Dabusu. The 636-bp full-length gene encodes a polypeptide of 211 amino acid residues that is closely related with putative GDSL family lipases from Alkalibacterium and Enterococcus. The gene was successfully expressed in E. coli, and the recombinant protein (rEstSL3) was...
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A gene encoding a novel organic solvent-tolerant alkaline lipase, lipS (GenBank ID JQ071496), was cloned from cold-adapted Pseudomonas mandelii. Recombinant LipS was expressed in Escherichia coli as a 32-kDa soluble protein and was purified by standard procedures. It maintained more than 80% of its activity under alkaline conditions, pH 8-10.5, with an apparent optimum temperature range of 40-5...
متن کاملCharacterization of a New Cold-Adapted and Salt-Activated Polysaccharide Lyase Family 7 Alginate Lyase from Pseudoalteromonas sp. SM0524
Marine bacterial alginate lyases play a role in marine alginate degradation and carbon cycling. Although a large number of alginate lyases have been characterized, reports on alginate lyases with special characteristics are still rather less. Here, a gene alyPM encoding an alginate lyase of polysaccharide lyase family 7 (PL7) was cloned from marine Pseudoalteromonas sp. SM0524 and expressed in ...
متن کاملmolecular and catalytic characterization of acidophilic xylanase bacillus subtilis k40b
bacillus subtilis k40b was isolated from rice rhizospheres and its potential for production of xylanase was evaluated using biochemical methods. the gene for xylanase in b. subtilis k40b was amplified, sequenced and assigned to the ncbi genebank. the gene size was estimated to be 563 bp encoding 413 amino acids. comparison of the xylanase gene with reference sequences showed that the xylanase o...
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ژورنال
عنوان ژورنال: BioResources
سال: 2016
ISSN: 1930-2126
DOI: 10.15376/biores.11.4.8875-8889