Stable esterase, a process for the extraction thereof, and use thereof for cleaving acyclic monoterpenyl esters into their monoterpenols

Abstract

A novel esterase, cleaving acyclic monoterpenyl esters into their monoterpenols, has been detected in the crude enzymic preparation of palmarosa (Cymbopogon martinii) inflorescence. The extraction and assay condition for the enzyme has been standardized. The esterase enzyme has shown maximum activity in the alkaline pH range, with optimum temperature at 30° C. using geranyl acetate (acyclic monoterpenyl acetate) as substrate. Time course hydrolysis of geranyl acetate using crude enzymic preparation revealed that after 24 hours of incubation approximately 75% geranyl acetate was hydrolyzed. The crude esterase enzyme, when stored at 4° C., was quite stable for one week with 40% loss of activity. The enzyme also has the capability to hydrolyze other acyclic monoterpenyl esters such as geranyl formate and citronellyl acetate, which are normally present in several aromatic plant species.

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