Functional Characterization of a Novel Marine Microbial GDSL Lipase and Its Utilization in the Resolution of (±)-1-Phenylethanol
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A novel GDSL lipase (MT6) was cloned from the genome of Marinactinospora thermotolerans SCSIO 00652 identified from the South China Sea. MT6 showed its maximum identity of 59 % with a putative lipase from Nocardiopsis dassonville. MT6 was heterologously expressed in E. coli BL21(DE3) and further functionally characterized. MT6 could efficiently resolve racemic 1-phenylethanol and generate (R)-1-phenylethanol with high enantiomeric excess (99 %) and conversion rate (54 %) through transesterification reactions after process optimization. Our report was the first one report about the utilization of one GDSL lipase in the preparation of chiral chemicals by transesterification reactions, and the optical selectivity of MT6 was interestingly opposite to those of other common lipases. GDSL lipases represented by MT6 possess great potential for the generation of valuable chiral chemicals in industry.
KeywordsNovel GDSL lipase Kinetic resolution (R)-1-phenylethanol Opposite optical selectivity
We are grateful for the financial supports from the National Natural Science Foundation of China (No. 21302199), Strategic Priority Research Program of the Chinese Academy of Sciences (XDA11030404), Project “Engineering High-Performance Microorganisms for Advanced Bio-Based Manufacturing” from the Chinese Academy of Sciences (KGZD-EW-606) and Guangzhou Science and Technology Plan Projects (201510010012). We also would like to thank for the constant helping from Professor Jianhua Ju and Professor Changsheng Zhang.
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