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Lipase-catalyzed transesterification of ethyl ferulate with triolein in solvent-free medium

Paper ID Volume ID Publish Year Pages File Format Full-Text
19393 43062 2011 6 PDF Available
Title
Lipase-catalyzed transesterification of ethyl ferulate with triolein in solvent-free medium
Abstract

The lipase-catalyzed transesterification of ethyl ferulate with triolein in a solvent-free medium was investigated. Transesterification was catalyzed by immobilized lipase from Candida antarctica (Novozym 435), to form ferulyl oleins, a mixture of ferulyl diolein and ferulyl monoolein. These ferulated esters can be widely used as natural antioxidant in both lipid containing food and cosmetic applications. External mass transfer limitations were lowest, when the agitation speed was higher than 180 rpm. A linear relationship between the initial reaction rate and enzyme load up to 10% demonstrated that the internal diffusion limitations could be minimized. The effects of various parameters on yields and rates of reaction were studied in the absence of mass transfer limitations. The initial reaction rate increased when the reaction temperature was raised in the range of 45–65 °C, further increase to 70 °C decreased the final yield to 48.9%. The value of activation energy was calculated as 65.04 kJ/mol based on the Arrhenius law. Under the most favorable conditions, a kinetic model based on the ping–pong bi–bi mechanism with triolein inhibition was found to fit the initial reaction rate data very well and the kinetic parameters were evaluated by non-linear regression analysis.

Research highlights▶ The transesterification of ethyl ferulate with triolein catalyzed by lipase Novozym 435 in a solvent-free medium was investigated through a one step reaction in which ethyl ferulate acts as acyl donor. ▶ The influence of external mass transfer limitation was negligible with a speed of agitation of 180 rpm. The internal diffusion limitations can be minimized. ▶ The yield increased with an increase in temperature from 45 °C to 65 °C. Based on the Arrhenius law the value of activation energy was calculated as 65.04 kJ/mol. ▶ Analyses of the kinetic data indicates that the transesterification can be described adequately by ping–pong bi–bi mechanism with triolein inhibition.

Keywords
Ferulyl oleins; Ethyl ferulate; Lipase; Kinetic model; Transesterification; Triolein
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Lipase-catalyzed transesterification of ethyl ferulate with triolein in solvent-free medium
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Publisher
Database: Elsevier - ScienceDirect
Journal: Food and Bioproducts Processing - Volume 89, Issue 4, October 2011, Pages 457–462
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us