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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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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. |
format | Online Article Text |
id | pubmed-6271819 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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