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

Journal Article · · Applied and Environmental Microbiology; (United States)
OSTI ID:5619023
; ; ; ; ;  [1];  [2]
  1. Osaka Univ., Matsubara City (Japan)
  2. Inst. for Fermentation, Osaka, Yodogawaku (Japan)

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).

OSTI ID:
5619023
Journal Information:
Applied and Environmental Microbiology; (United States), Vol. 58:1; ISSN 0099-2240
Country of Publication:
United States
Language:
English