Nano-organic supports for enzyme immobilization: Scopes and perspectives.

Enzyme immobilization Hybrid support Nano-organic support Thermal stability

Journal

Colloids and surfaces. B, Biointerfaces
ISSN: 1873-4367
Titre abrégé: Colloids Surf B Biointerfaces
Pays: Netherlands
ID NLM: 9315133

Informations de publication

Date de publication:
Aug 2021
Historique:
received: 23 01 2021
revised: 04 04 2021
accepted: 14 04 2021
pubmed: 2 5 2021
medline: 23 6 2021
entrez: 1 5 2021
Statut: ppublish

Résumé

A variety of organic nanomaterials and organic polymers are used for enzyme immobilization to increase enzymes stability and reusability. In this study, the effects of the immobilization of enzymes on organic and organic-inorganic hybrid nano-supports are compared. Immobilization of enzymes on organic support nanomaterials was reported to significantly improve thermal, pH and storage stability, acting also as a protection against metal ions inhibitory effects. In particular, the effects of enzyme immobilization on reusability, physical, kinetic and thermodynamic parameters were considered. Due to their biocompatibility with low health risks, organic support nanomaterials represent a good choice for the immobilization of enzymes. Organic nanomaterials, and especially organic-inorganic hybrids, can significantly improve the kinetic and thermodynamic parameters of immobilized enzymes compared to macroscopic supports. Moreover, organic nanomaterials are more environment friendly for medical applications, such as prodrug carriers and biosensors. Overall, organic hybrid nanomaterials are receiving increasing attention as novel nano-supports for enzyme immobilization and will be used extensively.

Identifiants

pubmed: 33932893
pii: S0927-7765(21)00218-6
doi: 10.1016/j.colsurfb.2021.111774
pii:
doi:

Substances chimiques

Enzymes, Immobilized 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

111774

Informations de copyright

Copyright © 2021 Elsevier B.V. All rights reserved.

Auteurs

Sahar Zahirinejad (S)

Department of Biology, Faculty of Basic Sciences, Shahrekord University, Sharekord, Iran.

Roohullah Hemmati (R)

Department of Biology, Faculty of Basic Sciences, Shahrekord University, Sharekord, Iran; Biotechnology Research Institute, Shahrekord University, Shahrekord, Iran. Electronic address: Roohullah.hemmati@sku.ac.ir.

Ahmad Homaei (A)

Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, Bandar Abbas, Iran.

Ali Dinari (A)

Research Center for Nanorobotics in Brain, Gwangju Institute of Science and Technology (GIST), 123 Cheomdan-gwagiro, Oryong-dong, Bukgu, 61005, Republic of Korea.

Saman Hosseinkhani (S)

Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

Soheila Mohammadi (S)

Pharmaceutical Sciences Research Center, Health Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran.

Fabio Vianello (F)

Department of Comparative Biomedicine and Food Science, University of Padova, Italy.

Articles similaires

Colorimetry Captopril Humans Alloys Limit of Detection
Anthraquinones Kinetics Water Purification Adsorption Thermodynamics
1.00
Humans Pyrophosphatases Protein Conformation Molecular Dynamics Simulation Kinetics

Discovery, characterization, and synthetic potential of two novel bacterial aryl-alcohol oxidases.

Paula Cinca-Fernando, Christian Ascaso-Alegre, Emma Sevilla et al.
1.00
Alcohol Oxidoreductases Catalytic Domain Crystallography, X-Ray Substrate Specificity Recombinant Proteins

Classifications MeSH