Diacylglycerol synthesis by enzymatic glycerolysis: Screening of commercially available lipases

Janni Brogaard Kristensen, X.B. Xu, Huiling Mu

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Seven lipases were screened for their ability to synthesize DAG in the glycerolysis of rapeseed oil. In batch reactions with free glycerol, the lipase carrier was of great importance for catalysis. Catalysis did not take place in reactions with lipases having hydrophilic carriers. The best DAG yield (approx. 60 wt%) was achieved with Novozym 435 and Lipase PS-D after 7 h, and an equilibrium was obtained. Stepwise addition of glycerol allowed catalysis with Novozym CALB L (immobilized) to take place in spite of the hydrophilic carrier; however, the DAG yield was only 19 wt%. This result suggests that glycerol forms a layer around the hydrophilic lipase particles, limiting contact between the lipases and the hydrophobic oil phase. With glycerol absorbed on silica gel, all lipases catalyzed the glycerolysis reaction. Faster conversion of TAG was obtained with Lipase PS-D, Lipase AK, and Lipase F-AP15 than in reactions with free glycerol, but the DAG yield remained approximately 60-65 wt%. Nonspecific lipases yielded more 1,3-DAG early in the reaction.
    Original languageEnglish
    JournalJournal of the american oil chemists society
    Volume82
    Issue number5
    Pages (from-to)329-334
    ISSN0003-021X
    Publication statusPublished - 2005

    Keywords

    • specificity of lipases
    • lipases
    • glycerolysis
    • lipase carrier
    • diacylglycerol
    • silica gel
    • glycerol

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