Optimized preparation and characterization of CLEA-lipase from cocoa pod husk

Cross-linked enzyme aggregate (CLEA) is easily prepared from crude enzyme and has many advantagesto the environment and it is considered as an economic method in the context of industrial biocatalysiscompared to free enzyme. In this work, a highly active and stable CLEA-lipase from cocoa pod husk (C...

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Main Authors:	Yusof, Faridah, Khanahmadi, Soofia, Amid, Azura, Mahmod, Safa Senan, Mahat, Mohd Khairizal
Format:	Article
Language:	English
Published:	Elsevier 2014
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/41566/ http://irep.iium.edu.my/41566/ http://irep.iium.edu.my/41566/ http://irep.iium.edu.my/41566/1/P_58.pdf

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spelling	iium-415662015-02-13T02:35:27Z http://irep.iium.edu.my/41566/ Optimized preparation and characterization of CLEA-lipase from cocoa pod husk Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan Mahat, Mohd Khairizal TP248.13 Biotechnology Cross-linked enzyme aggregate (CLEA) is easily prepared from crude enzyme and has many advantagesto the environment and it is considered as an economic method in the context of industrial biocatalysiscompared to free enzyme. In this work, a highly active and stable CLEA-lipase from cocoa pod husk (CPH)which is a by-product after removal of cocoa beans, were assayed for their hydrolytic activity and char-acterized under the optimum condition successfully. Face centered central composite design (FCCCD)under response surface methodology (RSM) was used to get the optimal conditions of the three signif-icant factors (concentration of ammonium sulfate, concentration of glutaraldehyde and concentrationof additive) to achieve higher enzyme activity of CLEA. From 20 runs, the highest activity recorded wasaround 9.407 U (83% recovered activity) under the condition of using 20% saturated ammonium sulfate,60 mM glutaraldehyde as cross-linker and 0.17 mM bovine serum albumin as feeder. Moreover, the opti-mal reaction temperature and pH value in enzymatic reaction for both crude enzyme and immobilizedwere found to be 45◦C at pH 8 and 60◦C at pH 8.2, respectively. A systematic study of the stability of CLEAand crude enzyme was taken with regards to temperature (25–60◦C) and pH (5–10) value and in bothfactors, CLEA-lipase showed more stability than free lipase. The Kmvalue of CLEA was higher comparedto free enzyme (0.55 mM vs. 0.08 mM). The CLEA retained more than 60% of the initial activity after sixcycles of reuse compared to free enzyme. The high stability and recyclability of CLEA-lipase from CPHmake it efficient for different industrial applications. Elsevier 2014 Article PeerReviewed application/pdf en http://irep.iium.edu.my/41566/1/P_58.pdf Yusof, Faridah and Khanahmadi, Soofia and Amid, Azura and Mahmod, Safa Senan and Mahat, Mohd Khairizal (2014) Optimized preparation and characterization of CLEA-lipase from cocoa pod husk. Journal of Biotechnology. ISSN 0168-1656 (In Press) http://www.sciencedirect.com/science/article/pii/S0168165614009912 http://dx.doi.org/10.1016/j.jbiotec.2014.11.015
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan Mahat, Mohd Khairizal Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
description	Cross-linked enzyme aggregate (CLEA) is easily prepared from crude enzyme and has many advantagesto the environment and it is considered as an economic method in the context of industrial biocatalysiscompared to free enzyme. In this work, a highly active and stable CLEA-lipase from cocoa pod husk (CPH)which is a by-product after removal of cocoa beans, were assayed for their hydrolytic activity and char-acterized under the optimum condition successfully. Face centered central composite design (FCCCD)under response surface methodology (RSM) was used to get the optimal conditions of the three signif-icant factors (concentration of ammonium sulfate, concentration of glutaraldehyde and concentrationof additive) to achieve higher enzyme activity of CLEA. From 20 runs, the highest activity recorded wasaround 9.407 U (83% recovered activity) under the condition of using 20% saturated ammonium sulfate,60 mM glutaraldehyde as cross-linker and 0.17 mM bovine serum albumin as feeder. Moreover, the opti-mal reaction temperature and pH value in enzymatic reaction for both crude enzyme and immobilizedwere found to be 45◦C at pH 8 and 60◦C at pH 8.2, respectively. A systematic study of the stability of CLEAand crude enzyme was taken with regards to temperature (25–60◦C) and pH (5–10) value and in bothfactors, CLEA-lipase showed more stability than free lipase. The Kmvalue of CLEA was higher comparedto free enzyme (0.55 mM vs. 0.08 mM). The CLEA retained more than 60% of the initial activity after sixcycles of reuse compared to free enzyme. The high stability and recyclability of CLEA-lipase from CPHmake it efficient for different industrial applications.
format	Article
author	Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan Mahat, Mohd Khairizal
author_facet	Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan Mahat, Mohd Khairizal
author_sort	Yusof, Faridah
title	Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
title_short	Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
title_full	Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
title_fullStr	Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
title_full_unstemmed	Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
title_sort	optimized preparation and characterization of clea-lipase from cocoa pod husk
publisher	Elsevier
publishDate	2014
url	http://irep.iium.edu.my/41566/ http://irep.iium.edu.my/41566/ http://irep.iium.edu.my/41566/ http://irep.iium.edu.my/41566/1/P_58.pdf
first_indexed	2023-09-18T20:59:30Z
last_indexed	2023-09-18T20:59:30Z
_version_	1777410528592789504

Optimized preparation and characterization of CLEA-lipase from cocoa pod husk

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