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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| Format: | Article |
| Language: | English |
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Elsevier
2015
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| Online Access: | http://irep.iium.edu.my/48226/ http://irep.iium.edu.my/48226/1/48226.pdf |
| _version_ | 1848783265313325056 |
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| 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 |
| building | IIUM Repository |
| collection | Online Access |
| 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.
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| first_indexed | 2025-11-14T16:18:36Z |
| format | Article |
| id | iium-48226 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T16:18:36Z |
| publishDate | 2015 |
| publisher | Elsevier |
| recordtype | eprints |
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| spelling | iium-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 PeerReviewed 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 |
| 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) |
| title | 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_short | 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) |
| topic | Q Science (General) TP248.13 Biotechnology |
| url | http://irep.iium.edu.my/48226/ http://irep.iium.edu.my/48226/ http://irep.iium.edu.my/48226/ http://irep.iium.edu.my/48226/1/48226.pdf |