Biochemical properties and structure analysis of a DAG-Like lipase from Malassezia globosa

International Journal of Molecular Sciences
Huan XuYonghua Wang

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-...Continue Reading

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Citations

Sep 27, 2016·Frontiers in Microbiology·Margarita SantiagoLoreto P Parra
Jun 6, 2016·World Journal of Microbiology & Biotechnology·Tayvich VorapreedaKobkul Laoteng
Feb 6, 2021·Applied Biochemistry and Biotechnology·Nutan MhetrasDigambar Gokhale
Apr 10, 2021·International Journal of Biological Macromolecules·Shahid AliYonghua Wang
Feb 3, 2021·Journal of Microbiology and Biotechnology·Minji ParkWon Hee Jung

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Methods Mentioned

BETA
glycosylation
Protein Assay

Software Mentioned

SignalP
BLAST
PyMOL
VERIFY
NetNGlyc
ClustalW2
ESPript
Discovery Studio

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