Molecular Cloning, Expression, and Characterization of a β-Agarase Gene, agaD, from a Marine Bacterium, Vibrio sp. Strain PO-303

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概要

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• The β-agarase-d gene (agaD) from a marine bacterium, Vibrio sp. strain PO-303, was cloned and expressed in Escherichia coli. The gene consists of 1,362 bp and encodes a protein of 453 amino acids with a predicted molecular weight of 50,824. The full length of agarase-d consists of a signal peptide, a glycoside hydrolase family 16 catalytic module (CM), and a carbohydrate binding module (CBM). The full length of agarase-d without the signal peptide (rAgaDΔfull), the catalytic module (rAgaDCM), or the CBM (rAgaDCBM) was expressed in E. coli as recombinant proteins. rAgaDCM exhibited higher enzyme activity (63.6 units/mg) than rAgaDΔfull (1.20 units/mg) against agarose. rAgaDCM hydrolyzed agar and porphyran to several oligosaccharides and acted on neoagarohexaose to produce neoagarotetraose and neoagarobiose, but did not act on neoagarotetraose. rAgaDCBM bound to agarose.

• 社団法人 日本農芸化学会の論文

著者

• Tamaru Yutaka

  Graduate School Of Bioresources Mie Univ.

• Dong Jinhua

  Graduate School of Bioresources, Mie University

• Araki Toshiyoshi

  Graduate School of Bioresources, Mie University

関連論文

• Molecular Cloning, Expression, and Characterization of a β-Agarase Gene, agaD, from a Marine Bacterium, Vibrio sp. Strain PO-303
• Supplemental effect of Porphyra spheroplasts on the growth and feed utilization of black sea bream
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• Cloning and Characterization of a β-1, 4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium, Vibrio sp. Strain MA-138
• Molecular Cloning, Expression, and Characterization of a β-Agarase Gene, agaD, from a Marine Bacterium, Vibrio sp. Strain PO-303

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