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

Cross-linked enzyme aggregate (CLEA), a new method of carrier free enzyme immobilization has many advantages and considered as an economical method in the context of industrial biocatalysis. In this research, a highly active and stable CLEA-lipase has been successfully prepared from cocoa pod husk (...

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Main Authors:	Khanahmadi, Soofia, Yusof, Faridah, Amid, Azura, Mahat, Mohd Khairizal
Format:	Article
Language:	English
Published:	Elsevier 2014
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/39215/ http://irep.iium.edu.my/39215/ http://irep.iium.edu.my/39215/ http://irep.iium.edu.my/39215/1/P55.pdf

id	iium-39215
recordtype	eprints
spelling	iium-392152017-06-20T02:59:56Z http://irep.iium.edu.my/39215/ Optimized preparation and characterization of CLEA-lipase from cocoa pod husk Khanahmadi, Soofia Yusof, Faridah Amid, Azura Mahat, Mohd Khairizal TP248.13 Biotechnology Cross-linked enzyme aggregate (CLEA), a new method of carrier free enzyme immobilization has many advantages and considered as an economical method in the context of industrial biocatalysis. In this research, a highly active and stable CLEA-lipase has been successfully prepared from cocoa pod husk (CPH), a by-product of the cocoa industry. Based on the Face Centered Central Composite Design (FCCCD) under Response Surface Methodology (RSM) using three important parameters, the optimal preparation condition of CLEA-lipase shows that the highest activity achieved is 9.407Uor 83% of the activity of the free lipase. It was prepared using 20% saturated (NH4)2SO4 as the precipitant, 60mMglutaraldehyde as the cross-linker and 0.169mM BSA as the feeder. The optimal reaction temperature and pH for both CLEA-lipase and free lipase differed, where they were 60 ◦C and 8.2 and 45 ◦C and 8 respectively. A systematic study of temperature and pH stability showed that CLEA-lipase is more stable than free lipase. Results also show that the prepared CLEA-lipase retained more than 50% of the initial activity after five repeated runs. The observed high stability and recyclability of CLEA-lipase prepared from CPH demonstrated that it has potential to be used in different industrial applications. Elsevier 2014 Article PeerReviewed application/pdf en http://irep.iium.edu.my/39215/1/P55.pdf Khanahmadi, Soofia and Yusof, Faridah and Amid, Azura and Mahat, Mohd Khairizal (2014) Optimized preparation and characterization of CLEA-lipase from cocoa pod husk. Journal of Biotechnology, 1855. S23-S24. ISSN 0168-1656 http://www.sciencedirect.com/science/journal/01681656 doi:10.1016/j.jbiotec.2014.07.079
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 Khanahmadi, Soofia Yusof, Faridah Amid, Azura Mahat, Mohd Khairizal Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
description	Cross-linked enzyme aggregate (CLEA), a new method of carrier free enzyme immobilization has many advantages and considered as an economical method in the context of industrial biocatalysis. In this research, a highly active and stable CLEA-lipase has been successfully prepared from cocoa pod husk (CPH), a by-product of the cocoa industry. Based on the Face Centered Central Composite Design (FCCCD) under Response Surface Methodology (RSM) using three important parameters, the optimal preparation condition of CLEA-lipase shows that the highest activity achieved is 9.407Uor 83% of the activity of the free lipase. It was prepared using 20% saturated (NH4)2SO4 as the precipitant, 60mMglutaraldehyde as the cross-linker and 0.169mM BSA as the feeder. The optimal reaction temperature and pH for both CLEA-lipase and free lipase differed, where they were 60 ◦C and 8.2 and 45 ◦C and 8 respectively. A systematic study of temperature and pH stability showed that CLEA-lipase is more stable than free lipase. Results also show that the prepared CLEA-lipase retained more than 50% of the initial activity after five repeated runs. The observed high stability and recyclability of CLEA-lipase prepared from CPH demonstrated that it has potential to be used in different industrial applications.
format	Article
author	Khanahmadi, Soofia Yusof, Faridah Amid, Azura Mahat, Mohd Khairizal
author_facet	Khanahmadi, Soofia Yusof, Faridah Amid, Azura Mahat, Mohd Khairizal
author_sort	Khanahmadi, Soofia
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/39215/ http://irep.iium.edu.my/39215/ http://irep.iium.edu.my/39215/ http://irep.iium.edu.my/39215/1/P55.pdf
first_indexed	2023-09-18T20:56:18Z
last_indexed	2023-09-18T20:56:18Z
_version_	1777410327432921088

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

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