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Open AccessArticle

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

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.
Int. J. Mol. Sci. 2014, 15(6), 10554-10566; https://doi.org/10.3390/ijms150610554
Received: 29 April 2014 / Revised: 15 May 2014 / Accepted: 22 May 2014 / Published: 12 June 2014
(This article belongs to the Section Materials Science)
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. View Full-Text
Keywords: Janibacter sp.; mono- and di-acylglycerol lipase; biochemical characterization; camellia oil Janibacter sp.; mono- and di-acylglycerol lipase; biochemical characterization; camellia oil
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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. https://doi.org/10.3390/ijms150610554

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. https://doi.org/10.3390/ijms150610554

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. https://doi.org/10.3390/ijms150610554

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