Purification and Characterization of a Family G/11 β-Xylanase from Streptomyces olivaceoviridis E-86

• Published in: Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2000-01, Vol.64 (2), p.447-451
• Main Authors: KANEKO, Satoshi, KUNO, Atsushi, MURAMATSU, Mizuho, IWAMATSU, Shinnosuke, KUSAKABE, Isao, HAYASHI, Kiyoshi
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Bacteriology; Base Sequence; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Chromatography, Liquid; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; family G/11 xylanase; Fundamental and applied biological sciences. Psychology; Metabolism. Enzymes; Microbiology; Miscellaneous; Mission oriented research; Molecular Sequence Data; purification; Sequence Homology, Amino Acid; Streptomyces - enzymology; Streptomyces lividans; Streptomyces olivaceoviridis; xylan binding domain; Xylan Endo-1,3-beta-Xylosidase; Xylosidases - chemistry; Xylosidases - isolation & purification; Xylosidases - metabolism
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.64.447

A β-xylanase (GXYN) was purified from the culture filtrate of Streptomyces olivaceoviridis E-86 by successive chromatography on DE-52, CM-Sepharose and Superose 12. The molecular mass of the xylanase was estimated to be 23 kDa, indicating that the enzyme consists of a catalytic domain only. The enzyme dis- played an optimum pH of 6, a temperature optimum of 60°C, a pH stability range from 2 to 11 and thermal stability up to 40°C. The N-terminal amino acid sequence of GXYN was A-T-V-I-T-T-N-Q-T-G-T-N-N-G-I-Y-Y-S-F-W-, and sharing a high degree of similarity with the N-terminal sequence of xylanases B and C from Streptomyces lividans, indicating GXYN belongs to family G/11 of glycoside hydrolases. GXYN was inferior to xylanase B from Streptomyces lividans in the hydrolysis of insoluble xylan because of its lack of a xylan binding domain.