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Int. J. Mol. Sci. 2016, 17(8), 1360; doi:10.3390/ijms17081360

Isolation and Characterization of a Glycosyl Hydrolase Family 16 β-Agarase from a Mangrove Soil Metagenomic Library

Key Laboratory of Tropical Marine Bio-Resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, China
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Academic Editor: Patrick C. Y. Woo
Received: 17 June 2016 / Revised: 28 July 2016 / Accepted: 15 August 2016 / Published: 19 August 2016
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
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Abstract

A mangrove soil metagenomic library was constructed and a β-agarase gene designated as AgaML was isolated by functional screening. The gene encoded for a 659-amino-acids polypeptide with an estimated molecular mass of 71.6 kDa. The deduced polypeptide sequences of AgaML showed the highest identity of 73% with the glycoside hydrolase family 16 β-agarase from Microbulbifer agarilyticus in the GenBank database. AgaML was cloned and highly expressed in Escherichia coli BL21(DE3). The purified recombinant protein, AgaML, showed optimal activity at 50 °C and pH 7.0. The kinetic parameters of Km and Vmax values toward agarose were 4.6 mg·mL−1 and 967.5 μM·min−1·mg−1, respectively. AgaML hydrolyzed the β-1,4-glycosidic linkages of agar to generate neoagarotetraose (NA4) and neoagarohexaose (NA6) as the main products. These characteristics suggest that AgaML has potential application in cosmetic, pharmaceuticals and food industries. View Full-Text
Keywords: agarase; metagenomic library; agar; neoagaro-oligosaccharides agarase; metagenomic library; agar; neoagaro-oligosaccharides
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MDPI and ACS Style

Mai, Z.; Su, H.; Zhang, S. Isolation and Characterization of a Glycosyl Hydrolase Family 16 β-Agarase from a Mangrove Soil Metagenomic Library. Int. J. Mol. Sci. 2016, 17, 1360.

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