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Cold-active lipases and esterases: a review on recombinant overexpression and other essential issues


Citation

Matinja, Adamu Idris and Ahmad Kamarudin, Nor Hafizah and Thean, Adam Chor Leow and Oslan, Siti Nurbaya and Mohamad Ali, Mohd Shukuri (2022) Cold-active lipases and esterases: a review on recombinant overexpression and other essential issues. International Journal of Molecular Sciences, 23 (23). art. no. 15394. pp. 1-17. ISSN 1661-6596; ESSN: 422-0067

Abstract

Cold environments characterised by diverse temperatures close to or below the water freezing point dominate about 80% of the Earth’s biosphere. One of the survival strategies adopted by microorganisms living in cold environments is their expression of cold-active enzymes that enable them to perform an efficient metabolic flux at low temperatures necessary to thrive and reproduce under those constraints. Cold-active enzymes are ideal biocatalysts that can reduce the need for heating procedures and improve industrial processes’ quality, sustainability, and cost-effectiveness. Despite their wide applications, their industrial usage is still limited, and the major contributing factor is the lack of complete understanding of their structure and cold adaptation mechanisms. The current review looked at the recombinant overexpression, purification, and recent mechanism of cold adaptation, various approaches for purification, and three-dimensional (3D) crystal structure elucidation of cold-active lipases and esterase.


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Official URL or Download Paper: https://www.mdpi.com/1422-0067/23/23/15394

Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Institute of Bioscience
Centre of Foundation Studies for Agricultural Science
DOI Number: https://doi.org/10.3390/ijms232315394
Publisher: MDPI
Keywords: Cold adaptation; 3D structure; Esterase; Lipase; Psychrophilic enzymes; Purification
Depositing User: Ms. Nur Faseha Mohd Kadim
Date Deposited: 11 Sep 2023 01:59
Last Modified: 11 Sep 2023 01:59
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/ijms232315394
URI: http://psasir.upm.edu.my/id/eprint/100718
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