Purification, properties, and partial amino acid sequences of thermostable xynalases from Streptomyces thermoviolaceus OPC-520
Article Abstract:
The isolation and characterization of two types of thermostable xylanases (1,4-beta-D-xyland xylanohydrolase) from Streptomyces thermoviolaceus OPC-520 was reported. The molecular weights, optimun pH levels, temperature and effects of various reagents on acivity were determined for both xylanases, designated as STX-II and STX-II. In addition, partial amino acid sequence analysis showed that STX-I has a 47% sequence analogy with the exoglucanase from Cellulomonas fimi while STX II indicated 46% sequence analogy with the xylanase from Bacillus pumilus.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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A novel beta-N-acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: gene cloning, expression, and assignment to family 3 of the glycosyl hydrolases
Article Abstract:
Research was conducted to examine the role of beta-N-acetylglucosaminidase gene (nagA) of Streptomyces thermoviolaceus in chitin degradation by strain OPC-520, its relationship to similar proteins isolated from other sources and the regulatory system involved in the induction of the enzyme. The molecular cloning and biochemical characterization of beta-N-acetylglucosaminidase is reported. Results demonstrate that NagA from S. thermoviolaceus OPC-520 is classified as a family 3 glycosyl hydrolase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Purification and properties of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520
Article Abstract:
The purification process andthe properties of the chitinase from the culture filtrate of Streptomyces thermoviolaceous OPC-520 are discussed. Succesive column chromatographies were used to purify the culture filtrate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis estimated the molecular mass of the chitinase. High sequence homology was found to exist between the enzyme and with chitinases from Serratia and Bacillus species.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
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