Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

For over a century, enzyme immobilisation has been proven to be a superior strategy to improve catalytic activity and reusability and ensure easy separation, easy operation, and reduced cost. Enzyme immobilisation allows for an easier separation of the enzyme from the reaction mixture, thus simplify...

Full description

Bibliographic Details
Published in:JOURNAL OF COMPOSITES SCIENCE
Main Authors: Mohidem, Nur Atikah; Mohamad, Mardawani; Rashid, Muhammad Usman; Norizan, Mohd Nurazzi; Hamzah, Fazlena; Mat, Hanapi bin
Format: Review
Language:English
Published: MDPI 2023
Subjects:
Online Access:https://www-webofscience-com.uitm.idm.oclc.org/wos/woscc/full-record/WOS:001131018100001
author Mohidem
Nur Atikah; Mohamad
Mardawani; Rashid
Muhammad Usman; Norizan
Mohd Nurazzi; Hamzah
Fazlena; Mat
Hanapi bin
spellingShingle Mohidem
Nur Atikah; Mohamad
Mardawani; Rashid
Muhammad Usman; Norizan
Mohd Nurazzi; Hamzah
Fazlena; Mat
Hanapi bin
Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
Materials Science
author_facet Mohidem
Nur Atikah; Mohamad
Mardawani; Rashid
Muhammad Usman; Norizan
Mohd Nurazzi; Hamzah
Fazlena; Mat
Hanapi bin
author_sort Mohidem
spelling Mohidem, Nur Atikah; Mohamad, Mardawani; Rashid, Muhammad Usman; Norizan, Mohd Nurazzi; Hamzah, Fazlena; Mat, Hanapi bin
Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
JOURNAL OF COMPOSITES SCIENCE
English
Review
For over a century, enzyme immobilisation has been proven to be a superior strategy to improve catalytic activity and reusability and ensure easy separation, easy operation, and reduced cost. Enzyme immobilisation allows for an easier separation of the enzyme from the reaction mixture, thus simplifying downstream processing. This technology protects the enzyme from degradation or inactivation by harsh reaction conditions, making it more robust and suitable to be used in various applications. Recent strategies of immobilisation methods, such as adsorption, cross-linking, entrapment or encapsulation, and covalent bonding, were critically reviewed. These strategies have shown promising results in improving enzyme stability, activity, and reusability in various applications. A recent development in enzyme immobilisation in nanomaterials and agrowaste renewable carriers is underlined in the current review. Furthermore, the use of nanomaterials and agrowaste carriers in enzyme immobilisation has gained significant attention due to their unique properties, such as high surface area, high mass transfer, biocompatibility, and sustainability. These materials offer promising outcomes for developing more efficient and sustainable immobilised enzymes. This state-of-the-art strategy allows for better control over enzyme reactions and enhances their reusability, leading to more cost-effective and environmentally friendly processes. The use of renewable materials also helps to reduce waste generation and promote the utilisation of renewable resources, further contributing to the development of a circular economy.
MDPI
2504-477X

2023
7
12
10.3390/jcs7120488
Materials Science
gold
WOS:001131018100001
https://www-webofscience-com.uitm.idm.oclc.org/wos/woscc/full-record/WOS:001131018100001
title Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
title_short Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
title_full Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
title_fullStr Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
title_full_unstemmed Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
title_sort Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers
container_title JOURNAL OF COMPOSITES SCIENCE
language English
format Review
description For over a century, enzyme immobilisation has been proven to be a superior strategy to improve catalytic activity and reusability and ensure easy separation, easy operation, and reduced cost. Enzyme immobilisation allows for an easier separation of the enzyme from the reaction mixture, thus simplifying downstream processing. This technology protects the enzyme from degradation or inactivation by harsh reaction conditions, making it more robust and suitable to be used in various applications. Recent strategies of immobilisation methods, such as adsorption, cross-linking, entrapment or encapsulation, and covalent bonding, were critically reviewed. These strategies have shown promising results in improving enzyme stability, activity, and reusability in various applications. A recent development in enzyme immobilisation in nanomaterials and agrowaste renewable carriers is underlined in the current review. Furthermore, the use of nanomaterials and agrowaste carriers in enzyme immobilisation has gained significant attention due to their unique properties, such as high surface area, high mass transfer, biocompatibility, and sustainability. These materials offer promising outcomes for developing more efficient and sustainable immobilised enzymes. This state-of-the-art strategy allows for better control over enzyme reactions and enhances their reusability, leading to more cost-effective and environmentally friendly processes. The use of renewable materials also helps to reduce waste generation and promote the utilisation of renewable resources, further contributing to the development of a circular economy.
publisher MDPI
issn 2504-477X

publishDate 2023
container_volume 7
container_issue 12
doi_str_mv 10.3390/jcs7120488
topic Materials Science
topic_facet Materials Science
accesstype gold
id WOS:001131018100001
url https://www-webofscience-com.uitm.idm.oclc.org/wos/woscc/full-record/WOS:001131018100001
record_format wos
collection Web of Science (WoS)
_version_ 1809678579116539904