Xylanases from Streptomyces cyaneus: their production, purification and characterization
نویسندگان
چکیده
منابع مشابه
Production, purification, characterization and over-expression of xylanases from actinomycetes.
Xylanases are a group of depolymerizing enzymes often used for the hydrolysis of xylan (present in hemicellulose) to monomeric sugars and comprise endo-xylanases (EC 3.2.1.8) and beta-xylosidases (EC 3.2.1.37). They often act in synergy with other enzymes for complete hydrolysis of hemicellulose. Xylanases find several industrial applications, for example in food and feed industries, paper and ...
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The endoxylanase complex from Streptomyces sp. strain B-12-2 was purified and characterized. The organism forms five distinct xylanases in the absence of significant cellulase activity when grown on oat spelt xylan. This is the largest number of endoxylanases yet reported for a streptomycete. On the basis of their physiochemical characteristics, they can be divided into two groups: the first gr...
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L-asparaginase is an anti-neoplastic agent used in the lymphoblastic leukaemia chemotherapy. In the present study a novel strain, Streptomyces gulbargensis was explored for the production of extra-cellular L-asparaginase using groundnut cake extract. The optimum pH, temperature, inoculum size and agitation speed for enzyme production were pH 8.5, 40°C, 1x10(8)spores/ml and 200 rev/min respectiv...
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By applying different classical and fast protein liquid chromatographic techniques, three xylanases (beta-1,4-d-xylan xylanhydrolase) were purified to homogeneity from the extracellular enzymatic complex of Bacillus polymyxa. The three enzymes (X(34)C, X(34)E, and X(22)) were small proteins of 34, 34, and 22 kDa and basic pIs 9.3, >9.3, and 9.0, respectively. X(34)C and X(34)E are closely relat...
متن کاملPurification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520.
Two types of xylanases (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) were isolated from the culture filtrate of a thermophilic actinomycete, Streptomyces thermoviolaceus OPC-520. The enzymes (STX-I and STX-II) were purified by chromatography with DEAE-Toyopearl 650 M, CM-Toyopearl 650 M, Sephadex G-75, Phenyl-Toyopearl 650 M, and Mono Q HR. The purified enzymes showed single bands on sodium do...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1993
ISSN: 0022-1287
DOI: 10.1099/00221287-139-9-1987