These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Transesterification activity of a novel lipase from Acinetobacter venetianus RAG-1.
    Author: Snellman EA, Colwell RR.
    Journal: Antonie Van Leeuwenhoek; 2008 Nov; 94(4):621-5. PubMed ID: 18720025.
    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.
    [Abstract] [Full Text] [Related] [New Search]