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Study of glucose ester synthesis by immobilized lipase from Candida sp.

Paper ID Volume ID Publish Year Pages File Format Full-Text
52157 46865 2008 6 PDF Available
Title
Study of glucose ester synthesis by immobilized lipase from Candida sp.
Abstract

A simple kinetic model derived from a Ping–Pong mechanism is proposed to describe the mono-esterification of glucose with stearic acid catalyzed by immobilized lipases from Candida sp. The mathematical expressions derived from this model have been tested with several sets of data obtained from reactions carried out at the different reactive temperatures. The predicted values provide very good fits of the experimental data for reactive temperatures from 35 to 45 °C, and the rate constants of the corresponding mechanistic reaction are obtained. The activation energy 19.4 kJ/mol is estimated for the formation of the monoester. The model also considers the kinetics of inactivation of the immobilized Candida sp. during the reaction. Reactive condition with 0.8 g molecular sieves/2 mL acetone at 35 or 40 °C for 48 h is good for the enzyme to keep its activity and for making the equilibrium produce glucose monoester of stearic acid.

Keywords
Glucose ester; Immobilized lipase; Candida sp.; Synthesis; Kinetic mechanism
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Study of glucose ester synthesis by immobilized lipase from Candida sp.
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Publisher
Database: Elsevier - ScienceDirect
Journal: Catalysis Communications - Volume 9, Issue 6, 31 March 2008, Pages 1369–1374
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Catalysis
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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