Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520
- Osaka Univ., Matsubara City (Japan)
- 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
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Related Subjects
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