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Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst

The modern biotechnology industry has a demand for macromolecules that can function in extreme environments. One example is cold-adapted proteases, possessing advantages such as maintaining high catalytic efficiency at low temperature and low energy input during production and inactivation. Meanwhil...

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Detalles Bibliográficos
Autores principales: Yang, Zhengfeng, Huang, Zhendi, Wu, Qian, Tang, Xianghua, Huang, Zunxi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10218192/
https://www.ncbi.nlm.nih.gov/pubmed/37239878
http://dx.doi.org/10.3390/ijms24108532
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author Yang, Zhengfeng
Huang, Zhendi
Wu, Qian
Tang, Xianghua
Huang, Zunxi
author_facet Yang, Zhengfeng
Huang, Zhendi
Wu, Qian
Tang, Xianghua
Huang, Zunxi
author_sort Yang, Zhengfeng
collection PubMed
description The modern biotechnology industry has a demand for macromolecules that can function in extreme environments. One example is cold-adapted proteases, possessing advantages such as maintaining high catalytic efficiency at low temperature and low energy input during production and inactivation. Meanwhile, cold-adapted proteases are characterised by sustainability, environmental protection, and energy conservation; therefore, they hold significant economic and ecological value regarding resource utilisation and the global biogeochemical cycle. Recently, the development and application of cold-adapted proteases have gained gaining increasing attention; however, their applications potential has not yet been fully developed, which has seriously restricted the promotion and application of cold-adapted proteases in the industry. This article introduces the source, related enzymology characteristics, cold resistance mechanism, and the structure-function relationship of cold-adapted proteases in detail. This is in addition to discussing related biotechnologies to improve stability, emphasise application potential in clinical medical research, and the constraints of the further developing of cold-adapted proteases. This article provides a reference for future research and the development of cold-adapted proteases.
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spelling pubmed-102181922023-05-27 Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst Yang, Zhengfeng Huang, Zhendi Wu, Qian Tang, Xianghua Huang, Zunxi Int J Mol Sci Review The modern biotechnology industry has a demand for macromolecules that can function in extreme environments. One example is cold-adapted proteases, possessing advantages such as maintaining high catalytic efficiency at low temperature and low energy input during production and inactivation. Meanwhile, cold-adapted proteases are characterised by sustainability, environmental protection, and energy conservation; therefore, they hold significant economic and ecological value regarding resource utilisation and the global biogeochemical cycle. Recently, the development and application of cold-adapted proteases have gained gaining increasing attention; however, their applications potential has not yet been fully developed, which has seriously restricted the promotion and application of cold-adapted proteases in the industry. This article introduces the source, related enzymology characteristics, cold resistance mechanism, and the structure-function relationship of cold-adapted proteases in detail. This is in addition to discussing related biotechnologies to improve stability, emphasise application potential in clinical medical research, and the constraints of the further developing of cold-adapted proteases. This article provides a reference for future research and the development of cold-adapted proteases. MDPI 2023-05-10 /pmc/articles/PMC10218192/ /pubmed/37239878 http://dx.doi.org/10.3390/ijms24108532 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Yang, Zhengfeng
Huang, Zhendi
Wu, Qian
Tang, Xianghua
Huang, Zunxi
Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
title Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
title_full Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
title_fullStr Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
title_full_unstemmed Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
title_short Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
title_sort cold-adapted proteases: an efficient and energy-saving biocatalyst
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10218192/
https://www.ncbi.nlm.nih.gov/pubmed/37239878
http://dx.doi.org/10.3390/ijms24108532
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