Triglyceride selectivity of immobilized Thermomyces lanuginosa lipase in interesterification

Torben Harald Rønne, Lars S. Pedersen, Xuebing Xu

    Research output: Contribution to journalJournal articleResearchpeer-review


    The triglyceride (fatty acid) selectivity of an immobilized lipase from Thermomyces lanuginosa (Lipozyme TL IM) was investigated in lipase-catalyzed interesterification reactions between two mono-acid TG in n-hexane. Tristearin (tri-C18:0) was used as a reference in a series of TG with saturated FA from tri-C4:0 to tri-C20:0, except for tri-C6:0, and in a series of unsaturated FA from tri-C18:1 to tri-C18:3. The quantification was performed by HPLC, and different methods of selectivity evaluation were used. None of the methods used showed any significant differences between the performances of the lipase on the different TG, indicating that Lipozyme TL IM is nonselective toward FA or TG in the system used. A response surface design was used to investigate the influence of water activities (aw) and reaction temperatures on the reactivity of Lipozyme TL IM with a system of tripalmitin (tri-C16:0) and trilaurin (tri-C12:0) in n-hexane. An increase in temperature (40 to 60°C) was found to affect the reactivity of the lipase significantly. The reactivity of Lipozyme TL IM was unaffected by the change in aw from 0.1130 to 0.5289. An increase in aw only led to an increase in FFA formation.
    Original languageEnglish
    JournalJournal of the american oil chemists society
    Pages (from-to)737-743
    Publication statusPublished - 2005


    Dive into the research topics of 'Triglyceride selectivity of immobilized Thermomyces lanuginosa lipase in interesterification'. Together they form a unique fingerprint.

    Cite this