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  • Title: Purification and characterization of a family G/11 beta-xylanase from Streptomyces olivaceoviridis E-86.
    Author: Kaneko S, Kuno A, Muramatsu M, Iwamatsu S, Kusakabe I, Hayashi K.
    Journal: Biosci Biotechnol Biochem; 2000 Feb; 64(2):447-51. PubMed ID: 10737210.
    Abstract:
    A beta-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 displayed an optimum pH of 6, a temperature optimum of 60 degrees C, a pH stability range from 2 to 11 and thermal stability up to 40 degrees 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.
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