Identification and Characterization of Cellobiose 2-Epimerases from Various Aerobes

• OJIMA Teruyo

  Nihon Shokuhin Kako Co., Ltd.

• SABURI Wataru

  Research Faculty of Agriculture, Hokkaido University

• YAMAMOTO Takeshi

  Nihon Shokuhin Kako Co., Ltd.

• MORI Haruhide

  Research Faculty of Agriculture, Hokkaido University

• MATSUI Hirokazu

  Research Faculty of Agriculture, Hokkaido University

Bibliographic Information

Other Title

• Identification and Characterization of an Inhibitor of Trichothecene 3-O-Acetyltransferase, TRI101, by the Chemical Array Approach
• Identification and Characterization of an Inhibitor of Trichothecene 3-<i>O</i>-Acetyltransferase, TRI101, by the Chemical Array Approach
• Identification and characterization of cellobiose 2-epimerase from various aerobes

Abstract

Cellobiose 2-epimerase (CE), found mainly in anaerobes, reversibly converts D-glucose residues at the reducing end of β-1,4-linked oligosaccharides to D-mannose residues. In this study, we characterized CE-like proteins from various aerobes (Flavobacterium johnsoniae NBRC 14942, Pedobacter heparinus NBRC 12017, Dyadobacter fermentans ATCC 700827, Herpetosiphon aurantiacus ATCC 23779, Saccharophagus degradans ATCC 43961, Spirosoma linguale ATCC 33905, and Teredinibacter turnerae ATCC 39867), because aerobes, more easily cultured on a large scale than anaerobes, are applicable in industrial processes. The recombinant CE-like proteins produced in Escherichia coli catalyzed epimerization at the C2 position of cellobiose, lactose, epilactose, and β-1,4-mannobiose, whereas N-acetyl-D-glucosamine, N-acetyl-D-mannosamine, D-glucose, and D-mannose were inert as substrates. All the CEs, except for P. heparinus CE, the optimum pH of which was 6.3, showed highest activity at weakly alkaline pH. CEs from D. fermentans, H. aurantiacus, and S. linguale showed higher optimum temperatures and thermostability than the other enzymes analyzed. The enzymes from D. fermentans, S. linguale, and T. turnerae showed significantly high k_cat and K_m values towards cellobiose and lactose. Especially, T. turnerae CE showed a very high k_cat value towards lactose, an attractive property for the industrial production of epilactose, which is carried out at high substrate concentrations.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 77 (1), 189-193, 2013

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• cellobiose 2-epimerase
• <i>N</i>-acetyl-<small>D</small>-glucosamine 2-epimerase
• substrate specificity
• epilactose
• epimerization

Details

• CRID: 1390001206478635904
• NII Article ID: 10031164711
• NII Article ID: 10031202751
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.120742
• DOI: 10.1271/bbb.130153
• COI: 1:STN:280:DC%2BC3s3ntVSrtA%3D%3D
• COI: 1:STN:280:DC%2BC3sbmsFaltA%3D%3D
• ISSN: 13476947
• ISSN: 09168451
• HANDLE: 2115/67508
• NDL BIB ID: 024897743
• NDL BIB ID: 024226819
• PubMed: 23291764
• PubMed: 24018674
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I024897743
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I024226819
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.120742
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.130153
• Text Lang: en
• Data Source:
  • JaLC
  • IRDB
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed