Antonie van Leeuwenhoek

, Volume 94, Issue 4, pp 621–625 | Cite as

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

  • Erick A. Snellman
  • Rita R. Colwell
Short Communication


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 · 10 μg protein) were measured at a w 0.86. Transesterification activity in hexane represented 32% of comparable hydrolytic activity in aqueous buffer.


Acinetobacter venetianus RAG-1 Lipase Transesterification 


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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  1. 1.Center of Marine BiotechnologyUniversity of Maryland Biotechnology InstituteBaltimoreUSA
  2. 2.Department of BiologyThe CitadelCharlestonUSA
  3. 3.Center of Bioinformatics and Computational BiologyInstitute for Advanced Computer Studies, University of MarylandCollege ParkUSA

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