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• W2059493399 abstract "The beta-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 (rAgaDDeltafull), 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 rAgaDDeltafull (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." @default.
• W2059493399 created "2016-06-24" @default.
• W2059493399 creator A5044773604 @default.
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• W2059493399 date "2007-01-23" @default.
• W2059493399 modified "2023-10-14" @default.
• W2059493399 title "Molecular Cloning, Expression, and Characterization of a β-Agarase Gene,<i>agaD</i>, from a Marine Bacterium,<i>Vibrio</i>sp. Strain PO-303" @default.
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• W2059493399 doi "https://doi.org/10.1271/bbb.60304" @default.
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