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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

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
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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Abstract

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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