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

  • KANEKO Satoshi
    National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries
  • KUNO Atsushi
    Department of Material and Biological Chemistry, Faculty of Science, Yamagata University National Institute for Advanced Interdisciplinary Research
  • MURAMATSU Mizuho
    Institute of Applied Biochemistry, University of Tsukuba
  • IWAMATSU Shinnosuke
    Department of Material and Biological Chemistry, Faculty of Science, Yamagata University
  • KUSAKABE Isao
    Institute of Applied Biochemistry, University of Tsukuba
  • HAYASHI Kiyoshi
    National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries

書誌事項

タイトル別名
  • Purification and Characterization of a Family G/11 .BETA.-Xylanase from Streptomyces olivaceoviridis E-86.
  • Purification and Characterization of a Family G 11 ベータ Xylanase from Streptomyces olivaceoviridis E 86
  • Purification and Characterization of a Family G/11 β-Xylanase from<i>Streptomyces olivaceoviridis</i>E-86
公開日
2000
資源種別
journal article
DOI
  • 10.1271/bbb.64.447
公開者
公益社団法人 日本農芸化学会

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説明

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.<br>

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