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Identification and Characterization of Cellobiose 2-Epimerases from Various Aerobes

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Title: Identification and Characterization of Cellobiose 2-Epimerases from Various Aerobes
Authors: Ojima, Teruyo Browse this author
Saburi, Wataru Browse this author →KAKEN DB
Yamamoto, Takeshi Browse this author
Mori, Haruhide Browse this author →KAKEN DB
Matsui, Hirokazu Browse this author →KAKEN DB
Keywords: cellobiose 2-epimerase
N-acetyl-D-glucosamine 2-epimerase
substrate specificity
epilactose
epimerization
Issue Date: Jan-2013
Publisher: Taylor & Francis
Journal Title: Bioscience, Biotechnology, and Biochemistry
Volume: 77
Issue: 1
Start Page: 189
End Page: 193
Publisher DOI: 10.1271/bbb.120742
PMID: 23291764
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.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on 1/2013, available online: http://wwww.tandfonline.com/10.1271/bbb.120742
Type: article (author version)
URI: http://hdl.handle.net/2115/67508
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 佐分利 亘

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