Biochemical Properties and Structure Analysis of a DAG-Like Lipase from Malassezia globosa
AbstractDiacylglycerol (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
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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.
Xu H, Lan D, Yang B, Wang Y. Biochemical Properties and Structure Analysis of a DAG-Like Lipase from Malassezia globosa. International Journal of Molecular Sciences. 2015; 16(3):4865-4879.Chicago/Turabian Style
Xu, Huan; Lan, Dongming; Yang, Bo; Wang, Yonghua. 2015. "Biochemical Properties and Structure Analysis of a DAG-Like Lipase from Malassezia globosa." Int. J. Mol. Sci. 16, no. 3: 4865-4879.