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Lipase‐catalysed biosynthesis of hexyl butyrate by direct esterification: optimisation by response surface methodology
Author(s) -
Shaw JeiFu,
Chang ShuWei,
Liao HuiFen,
Shieh ChwenJen
Publication year - 2003
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1588
Subject(s) - rhizomucor miehei , butyric acid , lipase , response surface methodology , chemistry , substrate (aquarium) , molar ratio , butyrate , hexanol , chromatography , catalysis , central composite design , organic chemistry , enzyme , triacylglycerol lipase , alcohol , biology , fermentation , ecology
The ability of immobilised lipase from Rhizomucor miehei (Lipozyme IM‐77) to catalyse the direct esterification of hexanol and butyric acid was investigated. Response surface methodology (RSM) and a four‐factor/five‐level central composite rotatable design (CCRD) were employed to evaluate the effects of synthesis parameters such as reaction time (2–10 h), temperature (25–65 °C), substrate molar ratio of hexanol to butyric acid (1:1–3:1) and enzyme amount (10–50%; 0.24–1.18 BAUN) on the percentage molar conversion of hexyl butyrate by direct esterification. All the parameters had significant effects on the percentage molar conversion. Based on ridge maximum analysis, the optimal conditions for synthesis were: reaction time 8.0 h, temperature 46.9 °C, substrate molar ratio 1:1.2 and enzyme amount 36.4% (0.87 BAUN). The predicted value was 100% and the actual experimental value 98.2% molar conversion. Copyright © 2003 Society of Chemical Industry