Studies on lipase-catalyzed synthesis of ethylglucoside lactate in non-aqueous phase.
- Author:
Ping ZOU
1
;
Dong-Zhi WEI
;
Mao-Bing TU
;
Hong ZHENG
Author Information
1. State Key Laboratory Bioreactor Engineering, East China University of Science & Technology, Shanghai 200237, China.
- Publication Type:Journal Article
- MeSH:
Candida;
enzymology;
Enzymes, Immobilized;
metabolism;
Esters;
metabolism;
Glucosides;
isolation & purification;
metabolism;
Kinetics;
Lactates;
isolation & purification;
metabolism;
Lactic Acid;
metabolism;
Lipase;
metabolism;
Substrate Specificity;
Temperature
- From:
Chinese Journal of Biotechnology
2002;18(1):94-98
- CountryChina
- Language:Chinese
-
Abstract:
Ethylglucoside lactate, a novel Alpha-Hydroxy Acids Derivative, was synthesized by transesterification in non-aqueous phase using immobilized lipase as biocatalyst. Based on the studies of the factors effecting initial rate and conversion under atmospheric pressure (solvent, acyl donor, different immobilized lipase, substrate concentration, enzyme concentration and temperature), the results show that solvent-free medium using butyllactate as acyl donor is suitable to the ester synthesis. The reaction conditions have been optimized as the following: the amount of enzyme = 75 g/L, the ethylglucoside concentration = 0.4 mol/L, 70 degrees C, 200 r/min, 50 h, which the conversion was 71%. A 90% conversion and a 60.7 mmol.L-1.h-1 initial rate can be obtained under reduced pressure, which the conditions are enzyme 75 g/L, ethylglucoside 0.35 mol/L, 65 degrees C, 200 r/min and 40 h. The product purified by extraction and SIO2 chromatography was identified by infrared spectroscopy and 1H NMR.
