Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase

Ethyl acetate is a versatile ester used as solvent and diluents. The conventional esterification reaction of ethanol and acetic acid was catalysed by sulphuric acid, H2SO4. Enzyme is a sustainable approach for the esterification reaction to produce ethyl acetate. In this study, the esterification...

Full description

Saved in:
Bibliographic Details
Main Author: Mohd Radzi, Nurul Adila
Format: Monograph
Language:English
Published: Universiti Sains Malaysia 2021
Subjects:
Online Access:http://eprints.usm.my/54734/1/Esterification%20Of%20Ethanol%20And%20Acetic%20Acid%20Catalysed%20By%20Immobilized%20Candida%20Rugosa%20Lipase_Nurul%20Adila%20Mohd%20Radzi_K4_2021_ESAR.pdf
http://eprints.usm.my/54734/
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.usm.eprints.54734
record_format eprints
spelling my.usm.eprints.54734 http://eprints.usm.my/54734/ Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase Mohd Radzi, Nurul Adila T Technology TP Chemical Technology Ethyl acetate is a versatile ester used as solvent and diluents. The conventional esterification reaction of ethanol and acetic acid was catalysed by sulphuric acid, H2SO4. Enzyme is a sustainable approach for the esterification reaction to produce ethyl acetate. In this study, the esterification reaction of ethanol and acetic acid catalysed by immobilized candida rugosa lipase (CRL) in n-hexane was optimized. The free CRL was immobilized by physical adsorption on support, Amberlite XAD7 which resulted in specific activity of 0.13 U/mg. The effect of reaction time, temperature, substrate molar ratio and enzyme loading were studied. Maximum conversion of 88% was attained at 2 hours of reaction time, temperature of 50°C, acetic acid to ethanol ratio of 0.5 and enzyme loading of 80 U. Next, the kinetic modelling of bi-substrate enzymatic transesterification of ethyl butyrate was studied using secondary data from research paper. The data was fitted to the rate equation of the kinetic model using non-linear regression to obtain the kinetic parameter. Based on the Lineweaver-Burk double reciprocal plot, the transesterification reaction follows ping-pong bi-bi mechanism with competitive inhibition by ethyl caprate. The kinetic parameters obtained was, Vmax = 1.1918 M, Km,A = 0.0117 M, Km,B = 0.1674, Ki,A = 0.1091 M, and Ki,B = 0.0031. Universiti Sains Malaysia 2021-06-01 Monograph NonPeerReviewed application/pdf en http://eprints.usm.my/54734/1/Esterification%20Of%20Ethanol%20And%20Acetic%20Acid%20Catalysed%20By%20Immobilized%20Candida%20Rugosa%20Lipase_Nurul%20Adila%20Mohd%20Radzi_K4_2021_ESAR.pdf Mohd Radzi, Nurul Adila (2021) Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase. Project Report. Universiti Sains Malaysia, Pusat Pengajian Kejuruteraan Kimia. (Submitted)
institution Universiti Sains Malaysia
building Hamzah Sendut Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Sains Malaysia
content_source USM Institutional Repository
url_provider http://eprints.usm.my/
language English
topic T Technology
TP Chemical Technology
spellingShingle T Technology
TP Chemical Technology
Mohd Radzi, Nurul Adila
Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase
description Ethyl acetate is a versatile ester used as solvent and diluents. The conventional esterification reaction of ethanol and acetic acid was catalysed by sulphuric acid, H2SO4. Enzyme is a sustainable approach for the esterification reaction to produce ethyl acetate. In this study, the esterification reaction of ethanol and acetic acid catalysed by immobilized candida rugosa lipase (CRL) in n-hexane was optimized. The free CRL was immobilized by physical adsorption on support, Amberlite XAD7 which resulted in specific activity of 0.13 U/mg. The effect of reaction time, temperature, substrate molar ratio and enzyme loading were studied. Maximum conversion of 88% was attained at 2 hours of reaction time, temperature of 50°C, acetic acid to ethanol ratio of 0.5 and enzyme loading of 80 U. Next, the kinetic modelling of bi-substrate enzymatic transesterification of ethyl butyrate was studied using secondary data from research paper. The data was fitted to the rate equation of the kinetic model using non-linear regression to obtain the kinetic parameter. Based on the Lineweaver-Burk double reciprocal plot, the transesterification reaction follows ping-pong bi-bi mechanism with competitive inhibition by ethyl caprate. The kinetic parameters obtained was, Vmax = 1.1918 M, Km,A = 0.0117 M, Km,B = 0.1674, Ki,A = 0.1091 M, and Ki,B = 0.0031.
format Monograph
author Mohd Radzi, Nurul Adila
author_facet Mohd Radzi, Nurul Adila
author_sort Mohd Radzi, Nurul Adila
title Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase
title_short Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase
title_full Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase
title_fullStr Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase
title_full_unstemmed Esterification Of Ethanol And Acetic Acid Catalysed By Immobilized Candida Rugosa Lipase
title_sort esterification of ethanol and acetic acid catalysed by immobilized candida rugosa lipase
publisher Universiti Sains Malaysia
publishDate 2021
url http://eprints.usm.my/54734/1/Esterification%20Of%20Ethanol%20And%20Acetic%20Acid%20Catalysed%20By%20Immobilized%20Candida%20Rugosa%20Lipase_Nurul%20Adila%20Mohd%20Radzi_K4_2021_ESAR.pdf
http://eprints.usm.my/54734/
_version_ 1744354464149536768
score 13.160551