Esterases as emerging biocatalysts: mechanistic insights, genomic and metagenomic, immobilization, and biotechnological applications

Rafeeq, H, Hussain, A, Shabbir, S, Ali, S, Bilal, M, Sher, F ORCID: https://orcid.org/0000-0003-2890-5912 and Iqbal, HMN, 2021. Esterases as emerging biocatalysts: mechanistic insights, genomic and metagenomic, immobilization, and biotechnological applications. Biotechnology and Applied Biochemistry. ISSN 0885-4513

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Abstract

Esterase enzymes are a family of hydrolases that catalyze the breakdown and formation of ester bonds. Esterases have gained a prominent position in today's world's industrial enzymes market. Due to their unique biocatalytic attributes, esterases contribute to environmentally sustainable design approaches, including biomass degradation, food and feed industry, dairy, clothing, agrochemical (herbicides, insecticides), bioremediation, biosensor development, anticancer, antitumor, gene therapy, and diagnostic purposes. Esterases can be isolated by a diverse range of mammalian tissues, animals, and microorganisms. The isolation of extremophilic esterases increases the interest of researchers in the extraction and utilization of these enzymes at the industrial level. Genomic, metagenomic, and immobilization techniques have opened innovative ways to extract esterases and utilize them for a longer time to take advantage of their beneficial activities. The current study discusses the types of esterases, metagenomic studies for exploring new esterases, and their biomedical applications in different industrial sectors.

Item Type:	Journal article
Publication Title:	Biotechnology and Applied Biochemistry
Creators:	Rafeeq, H., Hussain, A., Shabbir, S., Ali, S., Bilal, M., Sher, F. and Iqbal, H.M.N.
Publisher:	Wiley
Date:	26 October 2021
ISSN:	0885-4513
Identifiers:	Number Type 10.1002/bab.2277 DOI 1567640 Other
Divisions:	Schools > School of Science and Technology
Record created by:	Jeremy Silvester
Date Added:	23 Jul 2022 18:22
Last Modified:	26 Oct 2022 03:00
URI:	https://irep.ntu.ac.uk/id/eprint/46687

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