Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio

Many studies have been done on various species of insects to investigate their potential use in industries. This is because insects have high protein content which could be further manipulated. Due to its eating habit, Zophobas morio larvae, also known as supermeal worm has been shown to have high...

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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/51744/ http://irep.iium.edu.my/51744/ http://irep.iium.edu.my/51744/1/51744.pdf

id	iium-51744
recordtype	eprints
spelling	iium-517442016-08-22T06:06:47Z http://irep.iium.edu.my/51744/ Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio Easa, Muhammad Noor Yusof, Faridah Abd Halim, Amanatuzzakiah QP Physiology TP248.13 Biotechnology Many studies have been done on various species of insects to investigate their potential use in industries. This is because insects have high protein content which could be further manipulated. Due to its eating habit, Zophobas morio larvae, also known as supermeal worm has been shown to have high amylase activity. In this study, amylase from supermeal worm has been immobilized via Cross-Linked Enzyme Aggregates (CLEA) technique and its kinetic performance, evaluated. CLEA is one of the best immobilization technology in respect to enzyme stability and reusability. Kinetic performance of both free and CLEA-amylase were evaluated based on the Michaelis-Menten model. Results obtained based Hanes-Woolf, Lineweaver-Burk, Eadie-Hofstee and Hyperbolic Regression plots, showed that the kinetic parameters, Vmax and KM, changed upon immobilization. For CLEA-amylase, Hanes-Woolf plot had showed the best fitted model based on R2 with Vmax= 1.068 mM/min and KM= 0.182 mM. Lineweaver-Burk plot was used to obtain the kinetic parameters for free amylase, with Vmax and KM of 17.230 mM/min and 2.470 mM, respectively. The result from this study might open the new path in discovering the potential of using insects in industrial applications, for example, in detergent industry Kulliyah of Engineering, International Islamic University Malaysia 2016 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/51744/1/51744.pdf Easa, Muhammad Noor and Yusof, Faridah and Abd Halim, Amanatuzzakiah (2016) Kinetic performance 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 Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio
description	Many studies have been done on various species of insects to investigate their potential use in industries. This is because insects have high protein content which could be further manipulated. Due to its eating habit, Zophobas morio larvae, also known as supermeal worm has been shown to have high amylase activity. In this study, amylase from supermeal worm has been immobilized via Cross-Linked Enzyme Aggregates (CLEA) technique and its kinetic performance, evaluated. CLEA is one of the best immobilization technology in respect to enzyme stability and reusability. Kinetic performance of both free and CLEA-amylase were evaluated based on the Michaelis-Menten model. Results obtained based Hanes-Woolf, Lineweaver-Burk, Eadie-Hofstee and Hyperbolic Regression plots, showed that the kinetic parameters, Vmax and KM, changed upon immobilization. For CLEA-amylase, Hanes-Woolf plot had showed the best fitted model based on R2 with Vmax= 1.068 mM/min and KM= 0.182 mM. Lineweaver-Burk plot was used to obtain the kinetic parameters for free amylase, with Vmax and KM of 17.230 mM/min and 2.470 mM, respectively. The result from this study might open the new path in discovering the potential of using insects in industrial applications, for example, in detergent industry
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	Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio
title_short	Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio
title_full	Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio
title_fullStr	Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio
title_full_unstemmed	Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio
title_sort	kinetic performance 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/51744/ http://irep.iium.edu.my/51744/ http://irep.iium.edu.my/51744/1/51744.pdf
first_indexed	2023-09-18T21:13:20Z
last_indexed	2023-09-18T21:13:20Z
_version_	1777411398414893056

Kinetic performance of cross-linked enzyme aggregates (clea)-amylase from Zophobas morio

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