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 (...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2014
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| Online Access: | http://irep.iium.edu.my/39215/ http://irep.iium.edu.my/39215/1/P55.pdf |
| _version_ | 1848781740500320256 |
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| 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 |
| building | IIUM Repository |
| collection | Online Access |
| 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.
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| first_indexed | 2025-11-14T15:54:22Z |
| format | Article |
| id | iium-39215 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T15:54:22Z |
| publishDate | 2014 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| 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 |
| spellingShingle | TP248.13 Biotechnology Khanahmadi, Soofia Yusof, Faridah Amid, Azura Mahat, Mohd Khairizal Optimized preparation and characterization of CLEA-lipase from cocoa pod husk |
| title | 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_short | Optimized preparation and characterization of CLEA-lipase from cocoa pod husk |
| title_sort | optimized preparation and characterization of clea-lipase from cocoa pod husk |
| topic | TP248.13 Biotechnology |
| 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 |