Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate

Enzymes are preferred over chemical catalysts in a myriad of appli-cations owing to their high specificity, selectivity and moderate operating condi-tions. Enzymes in the soluble state are susceptible to instability and difficult in separation. Immobilization of enzyme onto a support increases its phy...

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Main Authors: Jameel, Ahmad Tariq, Mahmood, Labiba, Yusof, Faridah
Format: Book Chapter
Language:English
Published: Springer, Singapore 2020
Subjects:
Online Access:http://irep.iium.edu.my/83635/1/83635_Characterization%20of%20enzyme.pdf
http://irep.iium.edu.my/83635/
https://www.springer.com/gp/book/9789811547416
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Institution: Universiti Islam Antarabangsa Malaysia
Language: English
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spelling my.iium.irep.836352020-10-12T13:10:43Z http://irep.iium.edu.my/83635/ Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate Jameel, Ahmad Tariq Mahmood, Labiba Yusof, Faridah TP248.13 Biotechnology Enzymes are preferred over chemical catalysts in a myriad of appli-cations owing to their high specificity, selectivity and moderate operating condi-tions. Enzymes in the soluble state are susceptible to instability and difficult in separation. Immobilization of enzyme onto a support increases its physical and thermal stability, reusability and recovery from the reaction broth. Different support materials such as polymers, hydrogels, nanoparticles, nanofibers and nano-scaffolds are being used for enzyme immobilization. Carbon-based nanomaterials have gained high popularity among different support materials. Here, we present the research findings on the immobilization of β-glucosidase onto two novel support materials, i.e., glutaraldehyde-activated multi-walled carbon nanotubes (MWCNTs) and Ca-alginate beads. The relative merits of the two supports are compared in terms of the performance of the enzyme in each case. β-Glucosidase immobi-lized on glutaraldehyde-modified MWCNTs exhibited higher residual activity and stability compared to the enzyme encapsulated in Ca-alginate beads. Kinetic study shows a higher enzyme affinity for the substrate for enzyme immobilized onto MWCNT support compared to Ca-alginate. The overall results demonstrate that despite a general decrease in the enzyme activity due to immobilization, there is greater retention of activity of the immobilized enzyme upon multiple cycles of hydrolysis. This study provides distinct economic advantage of employing nanoparticles as support for enzyme immobilization for large-scale industrial applications. Springer, Singapore 2020 Book Chapter PeerReviewed application/pdf en http://irep.iium.edu.my/83635/1/83635_Characterization%20of%20enzyme.pdf Jameel, Ahmad Tariq and Mahmood, Labiba and Yusof, Faridah (2020) Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate. In: Advances in nanotechnology and its applications. Springer, Singapore, Singapore, pp. 1-19. ISBN 978-981-15-4741-6 https://www.springer.com/gp/book/9789811547416 10.1007/978-981-15-4742-3
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
language English
topic TP248.13 Biotechnology
spellingShingle TP248.13 Biotechnology
Jameel, Ahmad Tariq
Mahmood, Labiba
Yusof, Faridah
Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
description Enzymes are preferred over chemical catalysts in a myriad of appli-cations owing to their high specificity, selectivity and moderate operating condi-tions. Enzymes in the soluble state are susceptible to instability and difficult in separation. Immobilization of enzyme onto a support increases its physical and thermal stability, reusability and recovery from the reaction broth. Different support materials such as polymers, hydrogels, nanoparticles, nanofibers and nano-scaffolds are being used for enzyme immobilization. Carbon-based nanomaterials have gained high popularity among different support materials. Here, we present the research findings on the immobilization of β-glucosidase onto two novel support materials, i.e., glutaraldehyde-activated multi-walled carbon nanotubes (MWCNTs) and Ca-alginate beads. The relative merits of the two supports are compared in terms of the performance of the enzyme in each case. β-Glucosidase immobi-lized on glutaraldehyde-modified MWCNTs exhibited higher residual activity and stability compared to the enzyme encapsulated in Ca-alginate beads. Kinetic study shows a higher enzyme affinity for the substrate for enzyme immobilized onto MWCNT support compared to Ca-alginate. The overall results demonstrate that despite a general decrease in the enzyme activity due to immobilization, there is greater retention of activity of the immobilized enzyme upon multiple cycles of hydrolysis. This study provides distinct economic advantage of employing nanoparticles as support for enzyme immobilization for large-scale industrial applications.
format Book Chapter
author Jameel, Ahmad Tariq
Mahmood, Labiba
Yusof, Faridah
author_facet Jameel, Ahmad Tariq
Mahmood, Labiba
Yusof, Faridah
author_sort Jameel, Ahmad Tariq
title Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
title_short Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
title_full Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
title_fullStr Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
title_full_unstemmed Characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
title_sort characterization of enzyme immobilization on novel supports—multi-walled carbon nanotube and alginate
publisher Springer, Singapore
publishDate 2020
url http://irep.iium.edu.my/83635/1/83635_Characterization%20of%20enzyme.pdf
http://irep.iium.edu.my/83635/
https://www.springer.com/gp/book/9789811547416
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