A 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 super mealworm has been shown to have high a...

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Main Authors: Easa, Muhammad Noor, Yusof, Faridah, Abd Halim, Amanatuzzakiah
Format: Article
Language:English
Published: Faculty of Food Science & Technology, Universiti Putra Malaysia (UPM) 2017
Subjects:
Online Access:http://irep.iium.edu.my/59625/
http://irep.iium.edu.my/59625/
http://irep.iium.edu.my/59625/1/59625_A%20Kinetic%20performance%20of%20Cross-Linked.pdf
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spelling iium-596252018-03-13T06:46:05Z http://irep.iium.edu.my/59625/ A kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-amylase from Zophobas morio Easa, Muhammad Noor Yusof, Faridah Abd Halim, Amanatuzzakiah TP155 Chemical engineering 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 super mealworm has been shown to have high amylase activity. In this study, amylase from super mealworm has been immobilized via Cross-Linked Enzyme Aggregates (CLEA) technique and its kinetic performance, evaluated. CLEA is one of the best immobilization method with 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 on 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 showed the best-fitted model based on R2 with Vmax= 1.068 mM/min and KM= 0.182 mM, however, 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. Thus it is observed that upon immobilization, Vmax for amylase dropped appreciably, however, much lower substrate concentration is needed to saturate the enzymatic sites to reach its maximum catalytic efficiency. The result from this study might open the new path in discovering the potential use of insects in industrial applications, for example, making use of the recovered enzymes in the detergent industry. Faculty of Food Science & Technology, Universiti Putra Malaysia (UPM) 2017-12 Article PeerReviewed application/pdf en http://irep.iium.edu.my/59625/1/59625_A%20Kinetic%20performance%20of%20Cross-Linked.pdf Easa, Muhammad Noor and Yusof, Faridah and Abd Halim, Amanatuzzakiah (2017) A kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-amylase from Zophobas morio. International Food Research Journal (IFRJ), 24 (Suppl.). S320-S324. E-ISSN 2231-7546 http://www.ifrj.upm.edu.my/24%20(07)%202017%20supplementary/(10)%20R1.pdf
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic TP155 Chemical engineering
TP248.13 Biotechnology
spellingShingle TP155 Chemical engineering
TP248.13 Biotechnology
Easa, Muhammad Noor
Yusof, Faridah
Abd Halim, Amanatuzzakiah
A 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 super mealworm has been shown to have high amylase activity. In this study, amylase from super mealworm has been immobilized via Cross-Linked Enzyme Aggregates (CLEA) technique and its kinetic performance, evaluated. CLEA is one of the best immobilization method with 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 on 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 showed the best-fitted model based on R2 with Vmax= 1.068 mM/min and KM= 0.182 mM, however, 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. Thus it is observed that upon immobilization, Vmax for amylase dropped appreciably, however, much lower substrate concentration is needed to saturate the enzymatic sites to reach its maximum catalytic efficiency. The result from this study might open the new path in discovering the potential use of insects in industrial applications, for example, making use of the recovered enzymes in the detergent industry.
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 A kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-amylase from Zophobas morio
title_short A kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-amylase from Zophobas morio
title_full A kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-amylase from Zophobas morio
title_fullStr A kinetic performance of Cross-Linked Enzyme Aggregates (CLEA)-amylase from Zophobas morio
title_full_unstemmed A 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 Faculty of Food Science & Technology, Universiti Putra Malaysia (UPM)
publishDate 2017
url http://irep.iium.edu.my/59625/
http://irep.iium.edu.my/59625/
http://irep.iium.edu.my/59625/1/59625_A%20Kinetic%20performance%20of%20Cross-Linked.pdf
first_indexed 2023-09-18T21:24:28Z
last_indexed 2023-09-18T21:24:28Z
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