Transesterification activity of a novel lipase from Acinetobacter venetianus RAG-1

Antonie van Leeuwenhoek
Erick A Snellman, Rita R Colwell

Abstract

Transesterification activity and the industrial potential of a novel lipase prepared from Acinetobacter ventiatus RAG-1 were evaluated. Purified lipase samples were dialyzed against pH 9.0 buffer in a single optimization step prior to lyophilization. The enzyme and organic phase were pre-equilibrated (separately) to the same thermodynamic water activities (a (w)) ranging from a (w) 0.33 to 0.97. Production of 1-octyl butyrate by lipase-catalyzed transesterification of vinyl butyrate with 1-octanol in hexane was monitored by gas chromatography. Production of 1-octyl butyrate and initial rate of reaction depended on water activity. Product synthesis and rate of transesterification increased sharply with increase from a (w) 0.33 to 0.55. Highest product concentration (218 mM) and rate of reaction (18.7 micromol h(-1) . 10 microg protein) were measured at a (w) 0.86. Transesterification activity in hexane represented 32% of comparable hydrolytic activity in aqueous buffer.

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Citations

Sep 8, 2012·Applied Biochemistry and Biotechnology·Saisubramanian Nagarajan
Jun 23, 2009·Biotechnology Advances·Fariha HasanAbdul Hameed

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