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Int. J. Mol. Sci. 2014, 15(6), 10554-10566; doi:10.3390/ijms150610554
Article

Biochemical Properties of a New Cold-Active Mono- and Diacylglycerol Lipase from Marine Member Janibacter sp. Strain HTCC2649

1
,
1
,
1
,
2
 and
1,*
1 College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China 2 School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China
* Author to whom correspondence should be addressed.
Received: 29 April 2014 / Revised: 15 May 2014 / Accepted: 22 May 2014 / Published: 12 June 2014
(This article belongs to the Section Material Sciences and Nanotechnology)
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Abstract

Mono- and di-acylglycerol lipase has been applied to industrial usage in oil modification for its special substrate selectivity. Until now, the reported mono- and di-acylglycerol lipases from microorganism are limited, and there is no report on the mono- and di-acylglycerol lipase from bacteria. A predicted lipase (named MAJ1) from marine Janibacter sp. strain HTCC2649 was purified and biochemical characterized. MAJ1 was clustered in the family I.7 of esterase/lipase. The optimum activity of the purified MAJ1 occurred at pH 7.0 and 30 °C. The enzyme retained 50% of the optimum activity at 5 °C, indicating that MAJ1 is a cold-active lipase. The enzyme activity was stable in the presence of various metal ions, and inhibited in EDTA. MAJ1 was resistant to detergents. MAJ1 preferentially hydrolyzed mono- and di-acylglycerols, but did not show activity to triacylglycerols of camellia oil substrates. Further, MAJ1 is low homologous to that of the reported fungal diacylglycerol lipases, including Malassezia globosa lipase 1 (SMG1), Penicillium camembertii lipase U-150 (PCL), and Aspergillus oryzae lipase (AOL). Thus, we identified a novel cold-active bacterial lipase with a sn-1/3 preference towards mono- and di-acylglycerides for the first time. Moreover, it has the potential, in oil modification, for special substrate selectivity.
Keywords: Janibacter sp.; mono- and di-acylglycerol lipase; biochemical characterization; camellia oil Janibacter sp.; mono- and di-acylglycerol lipase; biochemical characterization; camellia oil
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Yuan, D.; Lan, D.; Xin, R.; Yang, B.; Wang, Y. Biochemical Properties of a New Cold-Active Mono- and Diacylglycerol Lipase from Marine Member Janibacter sp. Strain HTCC2649. Int. J. Mol. Sci. 2014, 15, 10554-10566.

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