Activity and stability of enzyme immobilized with ionic liquid based polymer materials

Enzyme immobilization methods are continuously being developed for a wide range of applications including biocatalysis and biotransformation. Compared to other immobilization methods, physical entrapment into a matrix is relatively simple and inexpensive, and causes a relatively small perturbation t...

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Main Authors: Moniruzzaman, M., Mahmood, H., Kamiya, N., Yusup, S., Goto, M.
Format: Article
Institution: Universiti Teknologi Petronas
Record Id / ISBN-0: utp-eprints.26133 /
Published: Taylor's University 2015
Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84922376387&partnerID=40&md5=388e528953acdd2fbf153b6e53fb9b7c
http://eprints.utp.edu.my/26133/
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spelling utp-eprints.261332021-08-30T06:50:02Z Activity and stability of enzyme immobilized with ionic liquid based polymer materials Moniruzzaman, M. Mahmood, H. Kamiya, N. Yusup, S. Goto, M. Enzyme immobilization methods are continuously being developed for a wide range of applications including biocatalysis and biotransformation. Compared to other immobilization methods, physical entrapment into a matrix is relatively simple and inexpensive, and causes a relatively small perturbation to the native enzyme structure and function. However, significant enzyme leaching from such biocatalytic polymers is the main constraint in using them for industrial levels. This study reports an ionic liquid (IL) polymer materials incorporating enzymes that can be used as active, stable and reusable biocatalysts to overcome the limitations. Lipase was microencapsulated in surfactant aggregates formed in an IL monomer or the solution of an IL monomer/IL and then incorporated into polymer frameworks through the free radical polymerization of an IL (1-vinyl-3-ethylimidazolium bis(trifluoromethylsulfonyl) amide (veimTf2N). The activity, stability and reusability of IL polymer materials containing lipase were evaluated using lipase-catalyzed hydrolysis of p-nitrophenyl butyrate (p-PNB) as a model reaction. It was found that lipase IL polymer materials exhibited excellent stability in aqueous solutions. More importantly, these biopolymer materials retained most of their activity after six reaction cycles. We firmly believe that enzyme containing IL polymeric materials developed in this study will provide several advantages over conventional polymer based methods for diverse enzymatic reactions. © School of Engineering, Taylor�s University. Taylor's University 2015 Article NonPeerReviewed https://www.scopus.com/inward/record.uri?eid=2-s2.0-84922376387&partnerID=40&md5=388e528953acdd2fbf153b6e53fb9b7c Moniruzzaman, M. and Mahmood, H. and Kamiya, N. and Yusup, S. and Goto, M. (2015) Activity and stability of enzyme immobilized with ionic liquid based polymer materials. Journal of Engineering Science and Technology, 10 . pp. 60-69. http://eprints.utp.edu.my/26133/
institution Universiti Teknologi Petronas
collection UTP Institutional Repository
description Enzyme immobilization methods are continuously being developed for a wide range of applications including biocatalysis and biotransformation. Compared to other immobilization methods, physical entrapment into a matrix is relatively simple and inexpensive, and causes a relatively small perturbation to the native enzyme structure and function. However, significant enzyme leaching from such biocatalytic polymers is the main constraint in using them for industrial levels. This study reports an ionic liquid (IL) polymer materials incorporating enzymes that can be used as active, stable and reusable biocatalysts to overcome the limitations. Lipase was microencapsulated in surfactant aggregates formed in an IL monomer or the solution of an IL monomer/IL and then incorporated into polymer frameworks through the free radical polymerization of an IL (1-vinyl-3-ethylimidazolium bis(trifluoromethylsulfonyl) amide (veimTf2N). The activity, stability and reusability of IL polymer materials containing lipase were evaluated using lipase-catalyzed hydrolysis of p-nitrophenyl butyrate (p-PNB) as a model reaction. It was found that lipase IL polymer materials exhibited excellent stability in aqueous solutions. More importantly, these biopolymer materials retained most of their activity after six reaction cycles. We firmly believe that enzyme containing IL polymeric materials developed in this study will provide several advantages over conventional polymer based methods for diverse enzymatic reactions. © School of Engineering, Taylor�s University.
format Article
author Moniruzzaman, M.
Mahmood, H.
Kamiya, N.
Yusup, S.
Goto, M.
spellingShingle Moniruzzaman, M.
Mahmood, H.
Kamiya, N.
Yusup, S.
Goto, M.
Activity and stability of enzyme immobilized with ionic liquid based polymer materials
author_sort Moniruzzaman, M.
title Activity and stability of enzyme immobilized with ionic liquid based polymer materials
title_short Activity and stability of enzyme immobilized with ionic liquid based polymer materials
title_full Activity and stability of enzyme immobilized with ionic liquid based polymer materials
title_fullStr Activity and stability of enzyme immobilized with ionic liquid based polymer materials
title_full_unstemmed Activity and stability of enzyme immobilized with ionic liquid based polymer materials
title_sort activity and stability of enzyme immobilized with ionic liquid based polymer materials
publisher Taylor's University
publishDate 2015
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-84922376387&partnerID=40&md5=388e528953acdd2fbf153b6e53fb9b7c
http://eprints.utp.edu.my/26133/
_version_ 1741197088662749184
score 11.62408

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