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Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals

Protease-producing bacteria play a vital role in degrading organic nitrogen in marine environments. However, the diversity of the bacteria and extracellular proteases has seldom been addressed, especially in communities of coral reefs. In this study, 136 extracellular protease-producing bacterial st...

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Autores principales: Su, Hongfei, Xiao, Zhenlun, Yu, Kefu, Huang, Qinyu, Wang, Guanghua, Wang, Yinghui, Liang, Jiayuan, Huang, Wen, Huang, Xueyong, Wei, Fen, Chen, Biao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7210813/
https://www.ncbi.nlm.nih.gov/pubmed/32411529
http://dx.doi.org/10.7717/peerj.9055
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author Su, Hongfei
Xiao, Zhenlun
Yu, Kefu
Huang, Qinyu
Wang, Guanghua
Wang, Yinghui
Liang, Jiayuan
Huang, Wen
Huang, Xueyong
Wei, Fen
Chen, Biao
author_facet Su, Hongfei
Xiao, Zhenlun
Yu, Kefu
Huang, Qinyu
Wang, Guanghua
Wang, Yinghui
Liang, Jiayuan
Huang, Wen
Huang, Xueyong
Wei, Fen
Chen, Biao
author_sort Su, Hongfei
collection PubMed
description Protease-producing bacteria play a vital role in degrading organic nitrogen in marine environments. However, the diversity of the bacteria and extracellular proteases has seldom been addressed, especially in communities of coral reefs. In this study, 136 extracellular protease-producing bacterial strains were isolated from seven genera of scleractinian corals from Luhuitou fringing reef, and their protease types were characterized. The massive coral had more cultivable protease-producing bacteria than branching or foliose corals. The abundance of cultivable protease-producing bacteria reached 10(6) CFU g(−1) of coral. Phylogenetic analysis of 16S rRNA gene sequences revealed that the isolates were assigned to 24 genera, from which 20 corresponded to the phyla Firmicutes and Proteobacteria. Bacillus and Fictibacillus were retrieved from all coral samples. Moreover, Vibrio and Pseudovibrio were most prevalent in massive or foliose coral Platygyra and Montipora. In contrast, 11 genera were each identified in only one isolate. Nearly all the extracellular proteases from the bacteria were serine proteases or metalloproteases; 45.83% of isolates also released cysteine or aspartic proteases. These proteases had different hydrolytic ability against different substrates. This study represents a novel insight on the diversity of cultivable protease-producing bacteria and their extracellular proteases in scleractinian corals.
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spelling pubmed-72108132020-05-14 Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals Su, Hongfei Xiao, Zhenlun Yu, Kefu Huang, Qinyu Wang, Guanghua Wang, Yinghui Liang, Jiayuan Huang, Wen Huang, Xueyong Wei, Fen Chen, Biao PeerJ Marine Biology Protease-producing bacteria play a vital role in degrading organic nitrogen in marine environments. However, the diversity of the bacteria and extracellular proteases has seldom been addressed, especially in communities of coral reefs. In this study, 136 extracellular protease-producing bacterial strains were isolated from seven genera of scleractinian corals from Luhuitou fringing reef, and their protease types were characterized. The massive coral had more cultivable protease-producing bacteria than branching or foliose corals. The abundance of cultivable protease-producing bacteria reached 10(6) CFU g(−1) of coral. Phylogenetic analysis of 16S rRNA gene sequences revealed that the isolates were assigned to 24 genera, from which 20 corresponded to the phyla Firmicutes and Proteobacteria. Bacillus and Fictibacillus were retrieved from all coral samples. Moreover, Vibrio and Pseudovibrio were most prevalent in massive or foliose coral Platygyra and Montipora. In contrast, 11 genera were each identified in only one isolate. Nearly all the extracellular proteases from the bacteria were serine proteases or metalloproteases; 45.83% of isolates also released cysteine or aspartic proteases. These proteases had different hydrolytic ability against different substrates. This study represents a novel insight on the diversity of cultivable protease-producing bacteria and their extracellular proteases in scleractinian corals. PeerJ Inc. 2020-05-06 /pmc/articles/PMC7210813/ /pubmed/32411529 http://dx.doi.org/10.7717/peerj.9055 Text en ©2020 Su et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Marine Biology
Su, Hongfei
Xiao, Zhenlun
Yu, Kefu
Huang, Qinyu
Wang, Guanghua
Wang, Yinghui
Liang, Jiayuan
Huang, Wen
Huang, Xueyong
Wei, Fen
Chen, Biao
Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
title Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
title_full Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
title_fullStr Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
title_full_unstemmed Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
title_short Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
title_sort diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals
topic Marine Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7210813/
https://www.ncbi.nlm.nih.gov/pubmed/32411529
http://dx.doi.org/10.7717/peerj.9055
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