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Int. J. Mol. Sci. 2015, 16(3), 4865-4879; doi:10.3390/ijms16034865

Biochemical Properties and Structure Analysis of a DAG-Like Lipase from Malassezia globosa

College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China
School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Christo Z. Christov
Received: 8 December 2014 / Revised: 21 January 2015 / Accepted: 9 February 2015 / Published: 4 March 2015
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Diacylglycerol (DAG)-like lipases are found to play an important role in the life sciences and industrial fields. A putative DAG-like lipase (MgMDL2) from Malassezia globosa was cloned and expressed in recombinant Pichia pastoris. The recombinant MgMDL2 was expressed as a glycosylated protein and purified into homogeneity by anion exchange chromatography. The activity of recombinant MgMDL2 was optimal at 15 °C and pH 6.0, and it keeps over 50% of relative activity at 5 °C, suggesting that MgMDL2 was a cold active lipase. MgMDL2 retained over 80% of initial activity after incubation at 30 and 40 °C for 2.5 h, but it was not stable at 50 °C. Incubation of methanol and ethanol at a concentration of 30% for 2 h did not affect the recombinant enzyme activity, while metal ions, including Ca2+, Mn2+ and Ni2+, sharply inhibited the MgMDL2 activity at 5 mM by 42%, 35% and 36%, respectively. MgMDL2 exhibited a preference for medium chain-length esters with highest activity toward p-nitrophenyl caprylate, while it was active on mono- and diacylglycerol but not on triacylglycerol, indicating that it was a typical DAG-like lipase. By homology modeling, Phe278 was predicted to be involved in the preference of MgMDL2 for monoacyl- and diacyl-glyceride substrates, but not triglycerides. View Full-Text
Keywords: DAG-like lipases; Malassezia globosa; cold active enzyme; glycosylation; structure analysis DAG-like lipases; Malassezia globosa; cold active enzyme; glycosylation; structure analysis

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MDPI and ACS Style

Xu, H.; Lan, D.; Yang, B.; Wang, Y. Biochemical Properties and Structure Analysis of a DAG-Like Lipase from Malassezia globosa. Int. J. Mol. Sci. 2015, 16, 4865-4879.

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