Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease

Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA’s main advantages. Results:...

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Main Authors:	Mahmod, Safa Senan, Yusof, Faridah, Jami, Mohammed Saedi, Khanahmadi, Soofia
Format:	Article
Language:	English
Published:	Springer Berlin Heidelberg 2016
Subjects:	Q Science (General) TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/48228/ http://irep.iium.edu.my/48228/ http://irep.iium.edu.my/48228/ http://irep.iium.edu.my/48228/1/P_73.pdf

id	iium-48228
recordtype	eprints
spelling	iium-482282017-01-11T02:44:50Z http://irep.iium.edu.my/48228/ Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease Mahmod, Safa Senan Yusof, Faridah Jami, Mohammed Saedi Khanahmadi, Soofia Q Science (General) TP248.13 Biotechnology Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA’s main advantages. Results: In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis–Menten models were used to determine the kinetic parameters i.e. Km and Vmax that helped in showing a significant difference after immobilization as compared to free protease. Conclusion: This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial applications. Springer Berlin Heidelberg 2016 Article PeerReviewed application/pdf en http://irep.iium.edu.my/48228/1/P_73.pdf Mahmod, Safa Senan and Yusof, Faridah and Jami, Mohammed Saedi and Khanahmadi, Soofia (2016) Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease. Bioresources and Bioprocessing, 3 (3). pp. 1-11. ISSN 2197-4365 http://link.springer.com/article/10.1186/s40643-015-0081-5 10.1186/s40643-015-0081-5
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
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 Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease
description	Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA’s main advantages. Results: In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis–Menten models were used to determine the kinetic parameters i.e. Km and Vmax that helped in showing a significant difference after immobilization as compared to free protease. Conclusion: This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial 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	Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease
title_short	Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease
title_full	Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease
title_fullStr	Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease
title_full_unstemmed	Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease
title_sort	optimizing the preparation conditions of cross-linked enzyme aggregates (clea)-protease
publisher	Springer Berlin Heidelberg
publishDate	2016
url	http://irep.iium.edu.my/48228/ http://irep.iium.edu.my/48228/ http://irep.iium.edu.my/48228/ http://irep.iium.edu.my/48228/1/P_73.pdf
first_indexed	2023-09-18T21:08:27Z
last_indexed	2023-09-18T21:08:27Z
_version_	1777411091672858624

Optimizing the preparation conditions of cross-linked enzyme aggregates (CLEA)-protease

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