Purification and Characterization of Laminaran Hydrolases from Trichoderma viride

• NOBE Rika

  <i>Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University</i>

• SAKAKIBARA Yoichi

  <i>Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University</i>

• FUKUDA Nobuhiro

  <i>Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University</i>

• YOSHIDA Naoto

  <i>Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University</i>

• OGAWA Kihachiro

  <i>Department of Food Technology, Faculty of Horticulture, Minami Kyushu University</i>

• SUIKO Masahito

  <i>Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University</i>

Bibliographic Information

Other Title

• Purification and Characterization of Laminaran Hydrolases from<i>Trichoderma viride</i>

Abstract

  At least three extracellular laminaran hydrolases which hydrolyzed laminaran (β-1,3:1,6-glucan) from Eisenia bicyclis were secreted in wheat bran solid medium by Trichoderma viride U-1. These three enzymes, lam AI, AII, and B, were purified to electrophoretic homogeneity. Their molecular masses were estimated to be 70.1, 70.4, and 45.0 kDa for lam AI, AII, and B, respectively, by SDS-PAGE. Whereas both lam AI and AII could hydrolyze laminarin from Laminaria digitata, lam AII showed higher activity against Laminaria laminarin rather than Eisenia laminaran. On the other hand, lam B preferentially hydrolyzed pustulan, a β-1,6-glucan. Laminarioligosaccharide was hydrolyzed by lam AI and AII but not B, whereas gentiooligosaccharide was hydrolyzed by only lam B. It showed that lam AI and AII were specific for β-1,3-linkages, but lam B was specific for β-1,6-linkages. These results indicated that T. viride U-1 has a multiple glucanolytic enzyme system.<br>

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 67 (6), 1349-1357, 2003

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• <i>Trichoderma viride</i>
• β-1,3-glucanase
• β-1,6-glucanase
• extracellular enzyme
• <i>Eisenia bicyclis</i>

Details

• CRID: 1390001206475075712
• NII Article ID: 110002694229
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.67.1349
• COI: 1:CAS:528:DC%2BD3sXltlensrw%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 6581791
• PubMed: 12843664
• Web Site: http://id.ndl.go.jp/bib/6581791
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6581791
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.67.1349
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed