Study of solvent hydrophobicity on lipase catalysed reaction esterification (CROSBI ID 481490)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Giacometti, Jasminka ; Milin, Čedomila ; Vasić-Rački, Đurđa ; Giacometti, Fabio
engleski
Study of solvent hydrophobicity on lipase catalysed reaction esterification
In an organic reaction medium enzymes display several interesting properties like enhanced (thermal) stability and different substrate and stereospecificitiesË1Í. Enzyme activities were performed at fixed substrate concentration and comparisons of the observed rates were made under examined conditionsË2Í. The effect of hydrophobic organic solvents, versus log P value, was studied in lipase catalysed esterification in a batch stirrer-tank reactor (BSTR). The reactions were carried out in equimolar ratio of glycerol and oleic acid and catalyzed by 6.67 mg/ml immobilized Mucor miehei lipase in a solvent system withË3Í and without molecular sieves. In the solvent system with molecular sieves, the temperature effect was determined. The assay of enzyme reaction was performed by measurement with the pH-stat method and simultaneously monitored by the chromatographic determination of oleic acid, monoolein and diolein. The reactions were followed by the determination of reaction conversions during 45 h. The differences in reaction rates were an effect of solvation or partitioning of the substrate and products. The solvents with log P Ž 3 (cyclohexane, heksane and isooctane) were most suitable for esterification of glycerol and oleic acid. The change of the system hydrophobicity, by using the tested solvents in the system with molecular sieves, influenced the initial rate conversion but had no effect on the final conversion. The lower log P showed higher differences in the concentration of mono- and diolein. The initial reaction rate of diolein production was higher but final monoolein concentrations were higher in all experiments. Solvent hydrophobicity had the same effect in the system without molecular sieves, but final conversions were lower.
enzymatic esterification; solvent hydrophobicity; lipase
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Podaci o prilogu
211-211-x.
2001.
objavljeno
Podaci o matičnoj publikaciji
The 5th International Symposium on Biocatalysis and Biotransformation (Biotrans 2001) : abstracts
Fessner, Wolf-Dieter
Darmstadt: Gesselschaft Deutscher Chemiker
Podaci o skupu
International Symposium on Biocatalysis and Biotransformation (5 ; 2001)
poster
02.09.2001-07.09.2001
Darmstadt, Njemačka