Novel lipase isolated from a Pseudomonas strain and its application in the synthesis of S(+)‐2‐O‐benzylglycerol‐1‐acetate

Isolation of a novel microbial lipase (EC 3.1.1.3) having specific catalytic activity for the synthesis of optically pure 2‐O‐benzylglycerol‐1‐acetate, the building block for the preparation of many β‐blockers, phospholipase A2 inhibitors and other biologically active compounds was the aim of this investigation. A Pseudomonas (strain G6), recently isolated from soil, produced an extracellular lipase. SDS–PAGE analysis showed that the lipase protein was a hexamer. The molecular weight of the sub‐units of the lipase protein were 10, 19, 29, 30, 47 and 53. The catalytic activity of the lipase was exploited for the synthesis of 2‐O‐benzylglycerol‐1‐acetate from 2‐O‐benzylglycerol through transesterification using vinyl acetate as acylating agent. High selectivity of the lipase towards the monoacetate product was demonstrated. A 97% enantiomeric excess (ee) of S(+)‐2‐O‐benzylglycerol‐1‐acetate was obtained when the reaction was carried out at room temperature with shaking. The lipase was highly active in anhydrous organic microenvironments and in non‐polar organic solvents with log P values above 2.5. © 2002 Society of Chemical Industry