Hydrolysis of lysophosphatidylcholines by a lipase from Malassezia globosa

卷:117

Wang, Xuping ; Xu, Huan ; Lan, Dongming ; Yang, Bo ; Wang, Yonghua

关键词: Hydrolysis;    Lysophosphatidylcholine;    Molecular docking;    Phosphatidylcholine;    SMG1;   

DOI  :  10.1002/ejlt.201400643

学科分类：食品科学和技术

【 摘 要 】

SMG1, a lipase produced by recombinant Pichia pastoris shows specific activity on mono- and diacylglycerol but not on triacylglycerol. To better understand the substrate selectivity of SMG1, the hydrolysis ability of SMG1 on PC and LPC were investigated. SMG1 was found to hydrolyze LPC, but has no activity toward PC. Besides, SMG1 lipase preferred 2-LPC to 1-LPC. Molecular docking simulation indicated that Phe278 and Leu103 contribute to reduce the size of the catalytic pocket, resulting in preventing PC access to the active site of SMG1. Our work may shed some light to understand the molecular basis of substrate selectivity of lipase with preference for DAGs. Practical applications: To our knowledge, there is no report on the application of lipases with preference for DAGs in phospholipids modification. This study could contribute to develop potential applications of SMG1 lipase in phospholipids industries. (A) Hydrolysis curve of 1-LPC, 2-LPC, and PC by SMG1 (B) Modeled 3-D structure of the SMG1-2-LPC complex (C) Modeled 3-D structure of the SMG1-1-LPC complex (D) F278 prevents PC enter into catalytic pocket.