Extreme cold environments are potential reservoirs of microorganisms producing unique and novel enzymes in response to environmental stress conditions. Such cold-adapted enzymes prove to be valuable tools in industrial biotechnology to meet the increasing demand for efficient biocatalysts. The inherent properties like high catalytic activity at low temperature, high specific activity and low activation energy make the cold-adapted enzymes well suited for application in various industries. The interest in this group of enzymes is expanding as they are the preferred alternatives to harsh chemical synthesis owing to their biodegradable and non-toxic nature. Irrespective of the multitude of applications, the use of cold-adapted enzymes at the industrial level is still limited. The current review presents the unique adaptive features and the role of cold-adapted enzymes in major industries like food, detergents, molecular biology and bioremediation. The review highlights the significance of technology i.e., metagenomics, metatranscriptomics and metaproteomics in enzyme bioprospection from extreme environments. It further points out the challenges in using cold-adapted enzymes at the industrial level and the innovations associated with novel enzyme prospection strategies. Documentations on cold-adapted enzymes and their applications are abundant; however, reports on the role of tools in exploring cold-adapted enzymes are still scarce. So, the review covers the aspect concerning the novel techniques for enzyme discovery from nature.
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http://dx.doi.org/10.1007/s13205-021-02929-y | DOI Listing |
Protein Expr Purif
January 2025
Manchester Institute of Biotechnology, Department of Chemistry, University of Manchester, 131 Princess St, Manchester, M1 7DN, United Kingdom. Electronic address:
Since their discovery in Mycobacterium tuberculosis (Mtb), F-dependent enzymes have been identified as both important drug targets and potential industrial biocatalysts, including for bioremediation of otherwise recalcitrant substrates. Mtb-FGD1, utilizes glucose 6-phosphate (G6P) as an electron donor for the reduction of F. Current expression systems for Mtb-FGD1 use Mycobacterium smegmatis as host, because of the tendency for it to form inclusion bodies in E.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland.
Cold-adapted microorganisms possess cold-active enzymes with potential applications in different industries and research areas. In this study, two genes encoding β-d-galactosidases belonging to Glycoside Hydrolase families 2 and 42 from the psychrotolerant Arctic bacterium sp. S3* were cloned, expressed in and , purified and characterized.
View Article and Find Full Text PDFAdv Sci (Weinh)
December 2024
School of Life Sciences, Northwestern Polytechnical University, 127 Youyi Road, Xi'an, 710072, China.
Developing novel cold-adapted nanozymes and elucidating their mechanisms of action remains a great challenge. Inspired by natural oxidases that utilize high-spin and high-valent metal-oxygen intermediates to achieve high efficiency at low temperatures, in this study, a series of MnO nanomaterials with varied valence and spin states are synthesized. The activity assay revealed that the oxygen vacancy-engineered ε-MnO nanozyme displayed excellent cold-adapted oxidase-like properties, and no observable activity loss is observed in the temperature range of -20 to 45 °C.
View Article and Find Full Text PDFInt J Food Microbiol
February 2025
College of Life Science, Shandong Normal University, Jinan 250358, China. Electronic address:
β-Galactosidases can be used to degrade lactose in milk to prepare lactose-free milk, which is sweeter than ordinary milk and suitable for people with lactose intolerance. The β-galactosidase gene (WcGal2809) was cloned from Weissella confusa SW1 and successfully expressed in Escherichia coli BL21(DE3). The active WcGal2809 was identified to be a heterodimer composed of two distinct proteins LacL (72.
View Article and Find Full Text PDFMar Drugs
November 2024
School of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
In the present review, we summarize genome mining of genomic data obtained from the psychrophilic Antarctic marine ciliate and its evolutionary-close mesophilic cosmopolitan counterpart . This analysis highlights adaptation strategies that are unique to the Antarctic ciliate, including antioxidant gene duplication and distinctive substitutions that may play roles in increased drug binding affinity and enzyme reaction rate in cold environments. Enzymes from psychrophiles are usually characterized by high activities and reaction rates at low temperatures compared with their counterparts from mesophiles and thermophiles.
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