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Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer

Proteases in the M23 family have specific activities toward elastin and bacterial peptidoglycan. The peptidoglycan-degrading property makes these proteases have potential as novel antimicrobials. Because M23 proteases cannot be maturely expressed in Escherichia coli, it is significant to improve the...

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Autores principales: Zhao, Hui-Lin, Yang, Jie, Chen, Xiu-Lan, Su, Hai-Nan, Zhang, Xi-Ying, Huang, Feng, Zhou, Bai-Cheng, Xie, Bin-Bin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271819/
https://www.ncbi.nlm.nih.gov/pubmed/24743935
http://dx.doi.org/10.3390/molecules19044779
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author Zhao, Hui-Lin
Yang, Jie
Chen, Xiu-Lan
Su, Hai-Nan
Zhang, Xi-Ying
Huang, Feng
Zhou, Bai-Cheng
Xie, Bin-Bin
author_facet Zhao, Hui-Lin
Yang, Jie
Chen, Xiu-Lan
Su, Hai-Nan
Zhang, Xi-Ying
Huang, Feng
Zhou, Bai-Cheng
Xie, Bin-Bin
author_sort Zhao, Hui-Lin
collection PubMed
description Proteases in the M23 family have specific activities toward elastin and bacterial peptidoglycan. The peptidoglycan-degrading property makes these proteases have potential as novel antimicrobials. Because M23 proteases cannot be maturely expressed in Escherichia coli, it is significant to improve the production of these enzymes in their wild strains. Pseudoalterin is a new M23 protease secreted by the deep-sea bacterium Pseudoalteromonas sp. CF6-2. In this study, the fermentation conditions of strain CF6-2 for pseudoalterin production were optimized using single factor experiments and response surface methodology to improve the enzyme yield. To reduce the fermentation cost, bovine artery powder instead of elastin was determined as a cheap and efficient inducer. Based on single factor experiments, artery powder content, culture temperature and culture time were determined as the main factors influencing pseudoalterin production and were further optimized by the central composite design. The optimal values of these factors were determined as: artery powder of 1.2%, culture temperature of 20.17 °C and culture time of 28.04 h. Under the optimized conditions, pseudoalterin production reached 100.02 ± 9.0 U/mL, more than twice of that before optimization. These results lay a good foundation for developing the biotechnological potential of pseudoalterin.
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spelling pubmed-62718192019-01-02 Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer Zhao, Hui-Lin Yang, Jie Chen, Xiu-Lan Su, Hai-Nan Zhang, Xi-Ying Huang, Feng Zhou, Bai-Cheng Xie, Bin-Bin Molecules Article Proteases in the M23 family have specific activities toward elastin and bacterial peptidoglycan. The peptidoglycan-degrading property makes these proteases have potential as novel antimicrobials. Because M23 proteases cannot be maturely expressed in Escherichia coli, it is significant to improve the production of these enzymes in their wild strains. Pseudoalterin is a new M23 protease secreted by the deep-sea bacterium Pseudoalteromonas sp. CF6-2. In this study, the fermentation conditions of strain CF6-2 for pseudoalterin production were optimized using single factor experiments and response surface methodology to improve the enzyme yield. To reduce the fermentation cost, bovine artery powder instead of elastin was determined as a cheap and efficient inducer. Based on single factor experiments, artery powder content, culture temperature and culture time were determined as the main factors influencing pseudoalterin production and were further optimized by the central composite design. The optimal values of these factors were determined as: artery powder of 1.2%, culture temperature of 20.17 °C and culture time of 28.04 h. Under the optimized conditions, pseudoalterin production reached 100.02 ± 9.0 U/mL, more than twice of that before optimization. These results lay a good foundation for developing the biotechnological potential of pseudoalterin. MDPI 2014-04-16 /pmc/articles/PMC6271819/ /pubmed/24743935 http://dx.doi.org/10.3390/molecules19044779 Text en © 2014 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Zhao, Hui-Lin
Yang, Jie
Chen, Xiu-Lan
Su, Hai-Nan
Zhang, Xi-Ying
Huang, Feng
Zhou, Bai-Cheng
Xie, Bin-Bin
Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer
title Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer
title_full Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer
title_fullStr Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer
title_full_unstemmed Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer
title_short Optimization of Fermentation Conditions for the Production of the M23 Protease Pseudoalterin by Deep-Sea Pseudoalteromonas sp. CF6-2 with Artery Powder as an Inducer
title_sort optimization of fermentation conditions for the production of the m23 protease pseudoalterin by deep-sea pseudoalteromonas sp. cf6-2 with artery powder as an inducer
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271819/
https://www.ncbi.nlm.nih.gov/pubmed/24743935
http://dx.doi.org/10.3390/molecules19044779
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