Purification, Characterization, and Subsite Affinities of<i>Thermoactinomyces vulgaris</i>R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases

• ICHIKAWA Kazuhiro

  Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

• TONOZUKA Takashi

  Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

• UOTSU-TOMITA Rie

  Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

• AKEBOSHI Hiromi

  Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

• NISHIKAWA Atsushi

  Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

• SAKANO Yoshiyuki

  Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

書誌事項

タイトル別名

• Purification, Characterization, and Subsite Affinities of Thermoactinomyces vulgaris R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases

抄録

A maltooligosaccharide-metabolizing enzyme from Thermoactinomyces vulgaris R-47 (TGA) homologous to glucoamylases does not degrade starch efficiently unlike most glucoamylases such as fungal glucoamylases (Uotsu-Tomita et al., Appl. Microbiol. Biotechnol., 56, 465–473 (2001)). In this study, we purified and characterized TGA, and determined the subsite affinities of the enzyme. The optimal pH and temperature of the enzyme are 6.8 and 60°C, respectively. Activity assays with 0.4% substrate showed that TGA was most active against maltotriose, but did not prefer soluble starch. Kinetic analysis using maltooligosaccharides ranging from maltose to maltoheptaose revealed that TGA has high catalytic efficiency for maltotriose and maltose. Based on the kinetics, subsite affinities were determined. The A₁+A₂ value of this enzyme was highly positive whereas A₄–A₆ values were negative and little affinity was detected at subsites 3 and 7. Thus, the subsite structure of TGA is different from that of any other GA. The results indicate that TGA is a metabolizing enzyme specific for small maltooligosaccharides.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 68 (2), 413-420, 2004

  公益社団法人 日本農芸化学会

キーワード

• <I>Thermoactinomyces vulgaris</I> R-47
• glucoamylase
• subsite affinity
• metabolism

詳細情報

• CRID: 1390001206473084800
• NII論文ID: 10013142121
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.68.413
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 6868502
• PubMed: 14981306
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6868502
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.68.413
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可