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

Abstract

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 54,000 and 33,000, respectively. The pIs were 4.2 (STX-I) and 8.0 (STX-II). The optimum pH levels for the activity of STX-I and STX-II were pH 7.0. The optimum temperature for the activity of STX-I was 70C, and that for the activity of STX-II was 60C. The enzymes were completely inhibited by N-bromosuccinimide. The enzymes degraded xylan, producing xylose and xylobiose as the predominant products, indicating that they were endoxylanases. STX-I showed high sequence homology with the exoglucanase from Cellulomonas fimi (47% homology), and STX-II showed high sequence homology with the xylanase from Bacillus pumilus (46% homology).

Authors:
; ; ; ; ;  [1];  [2]
  1. Osaka Univ., Matsubara City (Japan)
  2. Inst. for Fermentation, Osaka, Yodogawaku (Japan)
Publication Date:
OSTI Identifier:
5619023
Resource Type:
Journal Article
Journal Name:
Applied and Environmental Microbiology; (United States)
Additional Journal Information:
Journal Volume: 58:1; Journal ID: ISSN 0099-2240
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; STREPTOMYCES; ENZYME ACTIVITY; XYLANASE; BIOASSAY; AMINO ACID SEQUENCE; BIODEGRADATION; COMPARATIVE EVALUATIONS; FRACTIONATION; TAXONOMY; XYLANS; BACTERIA; BIOLOGY; CARBOHYDRATES; CHEMICAL REACTIONS; DECOMPOSITION; ENZYMES; EVALUATION; GLYCOSYL HYDROLASES; HEMICELLULOSE; HYDROLASES; MICROORGANISMS; MOLECULAR STRUCTURE; O-GLYCOSYL HYDROLASES; ORGANIC COMPOUNDS; POLYSACCHARIDES; PROTEINS; SACCHARIDES; SEPARATION PROCESSES; 550200* - Biochemistry

Citation Formats

Tsujibo, Hiroshi, Miyamoto, Katsushiro, Kuda, Takashi, Minami, Kazushi, Sakamoto, Takashi, Inamori, Yoshihiko, and Hasegawa, Toru. Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520. United States: N. p., 1992. Web.
Tsujibo, Hiroshi, Miyamoto, Katsushiro, Kuda, Takashi, Minami, Kazushi, Sakamoto, Takashi, Inamori, Yoshihiko, & Hasegawa, Toru. Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520. United States.
Tsujibo, Hiroshi, Miyamoto, Katsushiro, Kuda, Takashi, Minami, Kazushi, Sakamoto, Takashi, Inamori, Yoshihiko, and Hasegawa, Toru. 1992. "Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520". United States.
@article{osti_5619023,
title = {Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520},
author = {Tsujibo, Hiroshi and Miyamoto, Katsushiro and Kuda, Takashi and Minami, Kazushi and Sakamoto, Takashi and Inamori, Yoshihiko and Hasegawa, Toru},
abstractNote = {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 54,000 and 33,000, respectively. The pIs were 4.2 (STX-I) and 8.0 (STX-II). The optimum pH levels for the activity of STX-I and STX-II were pH 7.0. The optimum temperature for the activity of STX-I was 70C, and that for the activity of STX-II was 60C. The enzymes were completely inhibited by N-bromosuccinimide. The enzymes degraded xylan, producing xylose and xylobiose as the predominant products, indicating that they were endoxylanases. STX-I showed high sequence homology with the exoglucanase from Cellulomonas fimi (47% homology), and STX-II showed high sequence homology with the xylanase from Bacillus pumilus (46% homology).},
doi = {},
url = {https://www.osti.gov/biblio/5619023}, journal = {Applied and Environmental Microbiology; (United States)},
issn = {0099-2240},
number = ,
volume = 58:1,
place = {United States},
year = {Wed Jan 01 00:00:00 EST 1992},
month = {Wed Jan 01 00:00:00 EST 1992}
}