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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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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. |
format | Online Article Text |
id | pubmed-10218192 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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