Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio

Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique to date. In this study, amylase extract from Zophobas morio (supermeal worm) larvae was immobilized using acetone as the precipitant, glutaraldehyde as the cross-linker and bovine serum albumin as the...

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Main Authors:	Easa, Muhammad Noor, Yusof, Faridah, Abd Halim , Amanatuzzakiah
Format:	Conference or Workshop Item
Language:	English
Published:	Kulliyah of Engineering, International Islamic University Malaysia 2016
Subjects:	QP Physiology TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/51746/ http://irep.iium.edu.my/51746/ http://irep.iium.edu.my/51746/1/51746.pdf

id	iium-51746
recordtype	eprints
spelling	iium-517462016-08-22T06:31:53Z http://irep.iium.edu.my/51746/ Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah QP Physiology TP248.13 Biotechnology Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique to date. In this study, amylase extract from Zophobas morio (supermeal worm) larvae was immobilized using acetone as the precipitant, glutaraldehyde as the cross-linker and bovine serum albumin as the additive. The characteristics of the produced CLEA was compared to its’ soluble counterpart, in terms of pH and temperature optimum and stabilities. The results showed that CLEA and free amylase had optimum temperature at 55°C and 45°C, respectively. CLEA-amylase displayed greater stability against high temperature as compared to free enzyme which has lost most of its activity when the temperature was set beyond 45°C. At 65°C, CLEA-amylase still retained 73.2% of its activity. Results also showed that, CLEAamylase exhibited pH optimum at 11, while it is 7 for free enzyme. Similarly, CLEA-amylase more stable than the free form, over a wider range of pH, particularly at higher pH of 9, 10 and 11. Recyclability study showed that CLEA-amylase can retain 14.9% of its residual activity after 6 times of repeated uses. Since it is reusable, future works might include the evaluations of using CLEA-amylase at industrial level, remarkably in detergent applications. Kulliyah of Engineering, International Islamic University Malaysia 2016 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/51746/1/51746.pdf Easa, Muhammad Noor and Yusof, Faridah and Abd Halim , Amanatuzzakiah (2016) Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio. In: 4th International Conference on Biotechnology Engineering 2016 (ICBioE 2016), 25th-27th July 2016, Kuala Lumpur. http://www.iium.edu.my/icbioe/2016/
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	QP Physiology TP248.13 Biotechnology
spellingShingle	QP Physiology TP248.13 Biotechnology Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
description	Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique to date. In this study, amylase extract from Zophobas morio (supermeal worm) larvae was immobilized using acetone as the precipitant, glutaraldehyde as the cross-linker and bovine serum albumin as the additive. The characteristics of the produced CLEA was compared to its’ soluble counterpart, in terms of pH and temperature optimum and stabilities. The results showed that CLEA and free amylase had optimum temperature at 55°C and 45°C, respectively. CLEA-amylase displayed greater stability against high temperature as compared to free enzyme which has lost most of its activity when the temperature was set beyond 45°C. At 65°C, CLEA-amylase still retained 73.2% of its activity. Results also showed that, CLEAamylase exhibited pH optimum at 11, while it is 7 for free enzyme. Similarly, CLEA-amylase more stable than the free form, over a wider range of pH, particularly at higher pH of 9, 10 and 11. Recyclability study showed that CLEA-amylase can retain 14.9% of its residual activity after 6 times of repeated uses. Since it is reusable, future works might include the evaluations of using CLEA-amylase at industrial level, remarkably in detergent applications.
format	Conference or Workshop Item
author	Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah
author_facet	Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah
author_sort	Easa, Muhammad Noor
title	Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
title_short	Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
title_full	Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
title_fullStr	Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
title_full_unstemmed	Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
title_sort	characterization of cross-linked enzyme aggregates (clea)-amylase from zophobas morio
publisher	Kulliyah of Engineering, International Islamic University Malaysia
publishDate	2016
url	http://irep.iium.edu.my/51746/ http://irep.iium.edu.my/51746/ http://irep.iium.edu.my/51746/1/51746.pdf
first_indexed	2023-09-18T21:13:20Z
last_indexed	2023-09-18T21:13:20Z
_version_	1777411398702202880

Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio

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