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Triglyceride selectivity of immobilized Thermomyces lanuginosa lipase in interesterification
Author(s) -
Rønne Torben H.,
Pedersen Lars S.,
Xu Xuebing
Publication year - 2005
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-005-1136-8
Subject(s) - tripalmitin , interesterified fat , lipase , chemistry , chromatography , triglyceride , selectivity , triacylglycerol lipase , reactivity (psychology) , hexane , organic chemistry , biochemistry , catalysis , enzyme , cholesterol , medicine , alternative medicine , pathology
The triglyceride (fatty acid) selectivity of an immobilized lipase from Thermomyces lanuginosa (Lipozyme TL IM) was investigated in lipase‐catalyzed interesterification reactions between two nono‐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 ( a w ) 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 a w from 0.1130 to 0.5289. An increase in a w only led to an increase in FFA formation.