Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520

@article{Tsujibo1992PurificationPA,
  title={Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520},
  author={Hiroshi Tsujibo and Katsushiro Miyamoto and Takashi Kuda and Kosuke Minami and T Sakamoto and Tōru Hasegawa and Yoshihiko Inamori},
  journal={Applied and Environmental Microbiology},
  year={1992},
  volume={58},
  pages={371 - 375}
}
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 dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weights of STX-I and STX-II were 54… 
Gene Cloning, Expression, and Characterization of a Thermostable Xylanase from Nesterenkonia xinjiangensis CCTCC AA001025
TLDR
An endo-β-1,4-xylanase-encoding gene, xyn11NX, was cloned from Nesterenkonia xinjiangensis CCTCC AA001025 and expressed in Escherichia coli and exhibited a high degree of similarity with the xylanases from Streptomyces thermocyaneoviolaceus and Thermobifida fusca belonging to glycoside hydrolase family 11.
Thermostable xylanase from Streptomyces thermocyaneoviolaceus for optimal production of xylooligosaccharides
TLDR
A thermo stable xylanase was purified from Streptomyces thermocyaneoviolaceus M049 for the production of xylooligosaccharides from xylan and it was proposed that the XynB contained a 40 amino acid long signal peptide to the N-terminus.
Cloning and sequence analysis of genes encoding xylanases and acetyl xylan esterase from Streptomyces thermoviolaceus OPC-520
TLDR
Three genes encoding two types of xylanases and an acetyl xylan esterase from Streptomyces thermoviolaceus OPC-520 were cloned, and their DNA sequences were determined to demonstrate that the three enzymes contain two functional domains, a catalytic domain and a substrate-binding domain.
Cloning, Expression, and Characterization of a New Streptomyces sp. S27 Xylanase for Which Xylobiose is the Main Hydrolysis Product
  • Ning Li, P. Shi, B. Yao
  • Biology, Engineering
    Applied biochemistry and biotechnology
  • 2009
TLDR
The main hydrolysis product of xylan by XynBS27 was xylobiose, which was good for human health derived from its ability to modulate the intestinal function, and suggest that it may be a good candidate in a variety of industrial applications.
Purification and characterization of a new xylanase (APX-II) from the fungus Aureobasidium pullulans Y-2311-1
TLDR
Aureobasidium pullulans Y-2311-1 produced four major xylanases (EC 3.8, 4.0, 7.3, 9.9, and 9.4) and the sequence of the first 68 amino acid residues at the amino terminus showed homology to those of several other xylonases.
Cloning, expression, and characterization of protease-resistant xylanase from Streptomyces fradiae var. k11.
TLDR
The gene SfXyn10, which encodes a protease-resistant xylanase, was isolated using colony PCR screening from a genomic library of a feather-degrading bacterial strain and showed resistance to neutral and alkaline proteases.
Cloning, expression, and characterization of a new xylanase with broad temperature adaptability from Streptomyces sp. S9
A new xylanase gene, xynAS9, was cloned from Streptomyces sp. S9, which was isolated from Turpan Basin, China. The full-length gene consists of 1,395 bp and encodes 465 amino acids including 38
Cloning, Sequencing, and Expression of the Gene Encoding an Intracellular β-D-Xylosidase from Streptomyces thermoviolaceus OPC-520
TLDR
Thin-layer chromatography analysis showed that the intracellular β-xylosidase was induced when Streptomyces thermoviolaceus OPC-520 was grown at 50°C in a minimal medium containing xylan or xylooligosaccharides, but had no activity toward xylan.
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