Transesterification activity of a novel lipase from Acinetobacter venetianus RAG-1.
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.
Snellman
Erick A
EA
Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, MD, 21202, USA.
Colwell
Rita R
RR
D000150:Acinetobacter / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004951:Esterification; D006586:Hexanes / Q000378:metabolism; D008049:Lipase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D006586:Hexanes; C026385:n-hexane; D008049:Lipase