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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,*
Received: 29 April 2014; in revised form: 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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

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.

AMA Style

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. International Journal of Molecular Sciences. 2014; 15(6):10554-10566.

Chicago/Turabian Style

Yuan, Dongjuan; Lan, Dongming; Xin, Ruipu; Yang, Bo; Wang, Yonghua. 2014. "Biochemical Properties of a New Cold-Active Mono- and Diacylglycerol Lipase from Marine Member Janibacter sp. Strain HTCC2649." Int. J. Mol. Sci. 15, no. 6: 10554-10566.



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