Immobilized lipase Candida sp. 99-125 catalyzed methanolysis of glycerol trioleate: solvent effect.
The immobilized lipase Candida sp. 99-125 catalyzed methanolysis of glycerol trioleate was studied in twelve different solvents in order to deduce the solvent effect through an attempt to correlate the highest yield with such solvent properties as hydrophobicity (log P), dielectric constant (epsilon), and Hildebrand solubility parameter (delta). The results showed that the conversion of glycerol trioleate and yield of oleic acid methyl ester were quite dependent on the solvent. The catalyst lipase in various solvents also needed different optimum amount of water to keep its maximum activity, and generally this lipase in more hydrophobic solvents required more water. The correlation between the highest yield and log P value was found to be reasonable except deviation of data points of certain solvents, while no obvious correlation existed between the other two parameters, dielectric constant (epsilon) and Hildebrand solubility parameter (delta), and the enzyme activity. The study revealed that more hydrophobic solvents such as n-hexane or cyclohexane were more suitable solvents for Candida sp. 99-125 catalyzed transesterification of glycerol trioleate to oleic acid methyl ester.
Lu
Jike
J
Beijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China. ljk002004@163.com
Nie
Kaili
K
Wang
Fang
F
Tan
Tianwei
T
D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism*; D008697:Methane / Q000378:metabolism*; D012997:Solvents; D014304:Triolein / Q000378:metabolism*
D004800:Enzymes, Immobilized; D012997:Solvents; D014304:Triolein; D008049:Lipase; D008697:Methane