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KMID : 0613820080180050625
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Journal of Life Science
2008 Volume.18 No. 5 p.625 ~ p.630
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Cloning, Expression and Characterization of β-agarase Gene from a Marine Bacterium, Pseudoalteromonas sp. JT-6
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Tao Xue-Ying
Wu Jing
Kim Kyoung-Sook
Lee Young-Chun
Yu ZI-Niu
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Abstract
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gene (agaA6) encoding an extracellular agarase from a marine bacterium, Pseudoalteromonas sp. JT-6, was cloned, sequenced and expressed in Escherichia coli. It comprised an open reading frame of 1338 base pairs and encodes a protein of 445 amino acids with a predicted molecular weight of 50,150 daltons. The entire amino acid sequence of this agarase gene showed 99% identity with the agaA gene from Janthinobacterium sp. SY12. It consists of a signal peptide, a glycoside hydrolase family 16 β-agaras domain and a carbohydrate-binding domain. The recombinant agarase was overexpressed and purified to homogeneity. Enzyme activity analysis revealed that the optimum temperature and pH for the purified recombinant enzyme were around and 9.0. The enzyme was an endo-type β-agaras and hydrolyzed agarose to several oligosaccharides.
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KEYWORD
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Agarase, Pseudoalteromonas sp. JT-6, cloning, expression
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