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 nowadays. In this study, amylase extract from Zophobas morio (super mealworm) 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:	Article
Language:	English English
Published:	Faculty of Food Science & Technology, Universiti Putra Malaysia 2017
Subjects:	TP155 Chemical engineering TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/59626/ http://irep.iium.edu.my/59626/ http://irep.iium.edu.my/59626/17/59626_Characterization%20of%20Cross-Linked%20Enzyme%20Aggregates_article.pdf http://irep.iium.edu.my/59626/7/59626_Characterization%20of%20Cross-Linked%20enzyme_SCOPUS.pdf

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recordtype	eprints
spelling	iium-596262018-04-16T05:05:02Z http://irep.iium.edu.my/59626/ Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio Easa, Muhammad Noor Yusof, Faridah Abd Halim, Amanatuzzakiah TP155 Chemical engineering TP248.13 Biotechnology Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique nowadays. In this study, amylase extract from Zophobas morio (super mealworm) 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 were compared to the free soluble amylase, in terms of pH and temperature optimum and stabilities. The results displayed that CLEA and free amylase achieved an optimum temperature at 55°C and 45°C, respectively. CLEA-amylase also had showed greater stability against high temperature as compared to a free enzyme which had lost most of its activity when the temperature was set beyond 45°C. In comparison, at 65°C, CLEA-amylase still retained 73.2% of its activity. Results also revealed that CLEA-amylase has a pH optimum at 11, while it is pH 7 for free enzyme. Similarly, CLEA-amylase was 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 could 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 the industrial level, remarkably in detergent applications. Faculty of Food Science & Technology, Universiti Putra Malaysia 2017-12 Article PeerReviewed application/pdf en http://irep.iium.edu.my/59626/17/59626_Characterization%20of%20Cross-Linked%20Enzyme%20Aggregates_article.pdf application/pdf en http://irep.iium.edu.my/59626/7/59626_Characterization%20of%20Cross-Linked%20enzyme_SCOPUS.pdf Easa, Muhammad Noor and Yusof, Faridah and Abd Halim, Amanatuzzakiah (2017) Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio. International Food Research Journal, 24 (Suppl.). S335-S339. ISSN 1985-4668 E-ISSN 2231-7546 http://www.ifrj.upm.edu.my/24%20(07)%202017%20supplementary/(12)%20R1.pdf
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English
topic	TP155 Chemical engineering TP248.13 Biotechnology
spellingShingle	TP155 Chemical engineering 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 nowadays. In this study, amylase extract from Zophobas morio (super mealworm) 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 were compared to the free soluble amylase, in terms of pH and temperature optimum and stabilities. The results displayed that CLEA and free amylase achieved an optimum temperature at 55°C and 45°C, respectively. CLEA-amylase also had showed greater stability against high temperature as compared to a free enzyme which had lost most of its activity when the temperature was set beyond 45°C. In comparison, at 65°C, CLEA-amylase still retained 73.2% of its activity. Results also revealed that CLEA-amylase has a pH optimum at 11, while it is pH 7 for free enzyme. Similarly, CLEA-amylase was 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 could 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 the industrial level, remarkably in detergent applications.
format	Article
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	Faculty of Food Science & Technology, Universiti Putra Malaysia
publishDate	2017
url	http://irep.iium.edu.my/59626/ http://irep.iium.edu.my/59626/ http://irep.iium.edu.my/59626/17/59626_Characterization%20of%20Cross-Linked%20Enzyme%20Aggregates_article.pdf http://irep.iium.edu.my/59626/7/59626_Characterization%20of%20Cross-Linked%20enzyme_SCOPUS.pdf
first_indexed	2023-09-18T21:24:28Z
last_indexed	2023-09-18T21:24:28Z
_version_	1777412099390046208

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

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