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Microbial proteases and their applications

Proteases (proteinases or peptidases) are a class of hydrolases that cleave peptide chains in proteins. Endopeptidases are a type of protease that hydrolyze the internal peptide bonds of proteins, forming shorter peptides; exopeptidases hydrolyze the terminal peptide bonds from the C-terminal or N-t...

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Autores principales: Song, Peng, Zhang, Xue, Wang, Shuhua, Xu, Wei, Wang, Fei, Fu, Rongzhao, Wei, Feng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10537240/
https://www.ncbi.nlm.nih.gov/pubmed/37779686
http://dx.doi.org/10.3389/fmicb.2023.1236368
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author Song, Peng
Zhang, Xue
Wang, Shuhua
Xu, Wei
Wang, Fei
Fu, Rongzhao
Wei, Feng
author_facet Song, Peng
Zhang, Xue
Wang, Shuhua
Xu, Wei
Wang, Fei
Fu, Rongzhao
Wei, Feng
author_sort Song, Peng
collection PubMed
description Proteases (proteinases or peptidases) are a class of hydrolases that cleave peptide chains in proteins. Endopeptidases are a type of protease that hydrolyze the internal peptide bonds of proteins, forming shorter peptides; exopeptidases hydrolyze the terminal peptide bonds from the C-terminal or N-terminal, forming free amino acids. Microbial proteases are a popular instrument in many industrial applications. In this review, the classification, detection, identification, and sources of microbial proteases are systematically introduced, as well as their applications in food, detergents, waste treatment, and biotechnology processes in the industry fields. In addition, recent studies on techniques used to express heterologous microbial proteases are summarized to describe the process of studying proteases. Finally, future developmental trends for microbial proteases are discussed.
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spelling pubmed-105372402023-09-29 Microbial proteases and their applications Song, Peng Zhang, Xue Wang, Shuhua Xu, Wei Wang, Fei Fu, Rongzhao Wei, Feng Front Microbiol Microbiology Proteases (proteinases or peptidases) are a class of hydrolases that cleave peptide chains in proteins. Endopeptidases are a type of protease that hydrolyze the internal peptide bonds of proteins, forming shorter peptides; exopeptidases hydrolyze the terminal peptide bonds from the C-terminal or N-terminal, forming free amino acids. Microbial proteases are a popular instrument in many industrial applications. In this review, the classification, detection, identification, and sources of microbial proteases are systematically introduced, as well as their applications in food, detergents, waste treatment, and biotechnology processes in the industry fields. In addition, recent studies on techniques used to express heterologous microbial proteases are summarized to describe the process of studying proteases. Finally, future developmental trends for microbial proteases are discussed. Frontiers Media S.A. 2023-09-14 /pmc/articles/PMC10537240/ /pubmed/37779686 http://dx.doi.org/10.3389/fmicb.2023.1236368 Text en Copyright © 2023 Song, Zhang, Wang, Xu, Wang, Fu and Wei. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Song, Peng
Zhang, Xue
Wang, Shuhua
Xu, Wei
Wang, Fei
Fu, Rongzhao
Wei, Feng
Microbial proteases and their applications
title Microbial proteases and their applications
title_full Microbial proteases and their applications
title_fullStr Microbial proteases and their applications
title_full_unstemmed Microbial proteases and their applications
title_short Microbial proteases and their applications
title_sort microbial proteases and their applications
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10537240/
https://www.ncbi.nlm.nih.gov/pubmed/37779686
http://dx.doi.org/10.3389/fmicb.2023.1236368
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