Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)

This study focused on the production of a novel multi-CLEA comprising the enzyme activities of lipase and protease from fish viscera. A multi-CLEA is a single biocatalyst that can catalyze separate unrelated reactions, but these reactions can be conducted in one application. Tests pertaining to the...

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Main Authors: Mahmod, Safa Senan, Yusof, Faridah, Jami, Mohammed Saedi, Khanahmadi, Soofia
Format: Article
Language:English
Published: Elsevier 2015
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Online Access:http://irep.iium.edu.my/48226/1/48226.pdf
http://irep.iium.edu.my/48226/
http://www.sciencedirect.com/science/article/pii/S1359511315301021
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Institution: Universiti Islam Antarabangsa Malaysia
Language: English
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spelling my.iium.irep.482262016-07-17T08:43:36Z http://irep.iium.edu.my/48226/ Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA) Mahmod, Safa Senan Yusof, Faridah Jami, Mohammed Saedi Khanahmadi, Soofia Q Science (General) TP248.13 Biotechnology This study focused on the production of a novel multi-CLEA comprising the enzyme activities of lipase and protease from fish viscera. A multi-CLEA is a single biocatalyst that can catalyze separate unrelated reactions, but these reactions can be conducted in one application. Tests pertaining to the effect of various additives on the multi-CLEA’s activity were performed. Response Surface Methodology’s Face Centered Central Composite Design (FCCCD) was employed to optimize the preparation parameters of the multi-CLEA in an aqueous medium. It was found that 55% (w/v) of ammonium sulfate, 65 mM of glutaraldehyde, and 0.113 mM of bovine serum albumin were the optimum levels of additives to prepare the multi-CLEA with the protease and lipase recovery activity of 43.82% and 99.91%, respectively. Multi-CLEAs were found to retain an average of more than 34% of the initial activity after five consecutive batches for both enzymes. Finally, the multi-CLEA was utilized to catalyze two reactions: improved washing process and biodiesel production. The stain removal percentage of a commercial detergent was improved by 67.78% after adding multi-CLEA. In addition, the multi-CLEA catalyzed biodiesel production from vegetable oil with a percentage conversion of 51.7%. Such results demonstrated that the multi-CLEA is a promising catalyst for biotechnological applications. Elsevier 2015-12 Article REM application/pdf en http://irep.iium.edu.my/48226/1/48226.pdf Mahmod, Safa Senan and Yusof, Faridah and Jami, Mohammed Saedi and Khanahmadi, Soofia (2015) Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA). Process Biochemistry, 50 (12). pp. 2144-2157. ISSN 1359-5113 http://www.sciencedirect.com/science/article/pii/S1359511315301021 10.1016/j.procbio.2015.10.008
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
language English
topic Q Science (General)
TP248.13 Biotechnology
spellingShingle Q Science (General)
TP248.13 Biotechnology
Mahmod, Safa Senan
Yusof, Faridah
Jami, Mohammed Saedi
Khanahmadi, Soofia
Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)
description This study focused on the production of a novel multi-CLEA comprising the enzyme activities of lipase and protease from fish viscera. A multi-CLEA is a single biocatalyst that can catalyze separate unrelated reactions, but these reactions can be conducted in one application. Tests pertaining to the effect of various additives on the multi-CLEA’s activity were performed. Response Surface Methodology’s Face Centered Central Composite Design (FCCCD) was employed to optimize the preparation parameters of the multi-CLEA in an aqueous medium. It was found that 55% (w/v) of ammonium sulfate, 65 mM of glutaraldehyde, and 0.113 mM of bovine serum albumin were the optimum levels of additives to prepare the multi-CLEA with the protease and lipase recovery activity of 43.82% and 99.91%, respectively. Multi-CLEAs were found to retain an average of more than 34% of the initial activity after five consecutive batches for both enzymes. Finally, the multi-CLEA was utilized to catalyze two reactions: improved washing process and biodiesel production. The stain removal percentage of a commercial detergent was improved by 67.78% after adding multi-CLEA. In addition, the multi-CLEA catalyzed biodiesel production from vegetable oil with a percentage conversion of 51.7%. Such results demonstrated that the multi-CLEA is a promising catalyst for biotechnological applications.
format Article
author Mahmod, Safa Senan
Yusof, Faridah
Jami, Mohammed Saedi
Khanahmadi, Soofia
author_facet Mahmod, Safa Senan
Yusof, Faridah
Jami, Mohammed Saedi
Khanahmadi, Soofia
author_sort Mahmod, Safa Senan
title Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)
title_short Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)
title_full Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)
title_fullStr Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)
title_full_unstemmed Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)
title_sort development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-clea)
publisher Elsevier
publishDate 2015
url http://irep.iium.edu.my/48226/1/48226.pdf
http://irep.iium.edu.my/48226/
http://www.sciencedirect.com/science/article/pii/S1359511315301021
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