@article {38541,
	title = {Transesterification activity of a novel lipase from Acinetobacter venetianus RAG-1},
	journal = {Antonie van LeeuwenhoekAntonie van Leeuwenhoek},
	volume = {94},
	year = {2008},
	type = {10.1007/s10482-008-9276-5},
	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 μmol h-1 {\textperiodcentered} 10 μg protein) were measured at a w 0.86. Transesterification activity in hexane represented 32\% of comparable hydrolytic activity in aqueous buffer.},
	author = {Snellman, E. A. and Rita R. Colwell}
}
