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KMID : 0613820120220111545
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Journal of Life Science
2012 Volume.22 No. 11 p.1545 ~ p.1551
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Cloning, Expression, and Characterization of a Novel GH-16 β-Agarase from Agarivorans sp. JA-1
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Jeon Myong-Je
Kim A-Ram
Lee Dong-Geun
Lee Sang-Hyeon
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Abstract
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Authors report the glycoside hydrolase (GH) family 16 β-agarase from the strain of Agarivorans sp. JA-1, which authors previously stated as recombinant expression and characterization of GH-50 and GH-118 β-agarase. It comprised an open reading frame of 1,362 base pairs, which encodes a protein of 49,830 daltons consisting of 453 amino acid residues. Valuation of the total sequence showed that the enzyme has 98% nucleotide and 99% amino acid sequence similarities to those of GH-16 β-agarase from Pseudoalteromonas sp. CY24. The gene corresponding to a mature protein of 429 amino acids was recombinantly expressed in Escherichia coli, and the enzyme was purified to homogeneity by affinity chromatography. It showed maximal activity at 40℃ and pH 5.0, representing 67.6 units/mg. Thin layer chromatography revealed that mainly neoagarohexaose and neoagarotetraose were produced from agarose. The enzyme would be valuable for the industrial production of functional neoagarooligosaccharides.
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KEYWORD
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β-agarase, glycoside hydrolase family 16, Agarivorans, cloning, expression
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