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Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases

Carbohydrate-active enzymes (CAZymes) are an important characteristic of bacteria in marine systems. We herein describe the CAZymes of Paenibacillus algicola HB172198(T), a novel type species isolated from brown algae in Qishui Bay, Hainan, China. The genome of strain HB172198(T) is a 4,475,055 bp c...

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Autores principales: Huang, Huiqin, Zheng, Zhiguo, Zou, Xiaoxiao, Wang, Zixu, Gao, Rong, Zhu, Jun, Hu, Yonghua, Bao, Shixiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9227215/
https://www.ncbi.nlm.nih.gov/pubmed/35736191
http://dx.doi.org/10.3390/md20060388
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author Huang, Huiqin
Zheng, Zhiguo
Zou, Xiaoxiao
Wang, Zixu
Gao, Rong
Zhu, Jun
Hu, Yonghua
Bao, Shixiang
author_facet Huang, Huiqin
Zheng, Zhiguo
Zou, Xiaoxiao
Wang, Zixu
Gao, Rong
Zhu, Jun
Hu, Yonghua
Bao, Shixiang
author_sort Huang, Huiqin
collection PubMed
description Carbohydrate-active enzymes (CAZymes) are an important characteristic of bacteria in marine systems. We herein describe the CAZymes of Paenibacillus algicola HB172198(T), a novel type species isolated from brown algae in Qishui Bay, Hainan, China. The genome of strain HB172198(T) is a 4,475,055 bp circular chromosome with an average GC content of 51.2%. Analysis of the nucleotide sequences of the predicted genes shows that strain HB172198(T) encodes 191 CAZymes. Abundant putative enzymes involved in the degradation of polysaccharides were identified, such as alginate lyase, agarase, carrageenase, xanthanase, xylanase, amylases, cellulase, chitinase, fucosidase and glucanase. Four of the putative polysaccharide lyases from families 7, 15 and 38 were involved in alginate degradation. The alginate lyases of strain HB172198(T) exhibited the maximum activity 152 U/mL at 50 °C and pH 8.0, and were relatively stable at pH 7.0 and temperatures lower than 40 °C. The average degree of polymerization (DP) of the sodium alginate oligosaccharide (AOS) degraded by the partially purified alginate lyases remained around 14.2, and the thin layer chromatography (TCL) analysis indicated that it contained DP2-DP8 oligosaccharides. The complete genome sequence of P. algicola HB172198(T) will enrich our knowledge of the mechanism of polysaccharide lyase production and provide insights into its potential applications in the degradation of polysaccharides such as alginate.
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spelling pubmed-92272152022-06-25 Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases Huang, Huiqin Zheng, Zhiguo Zou, Xiaoxiao Wang, Zixu Gao, Rong Zhu, Jun Hu, Yonghua Bao, Shixiang Mar Drugs Article Carbohydrate-active enzymes (CAZymes) are an important characteristic of bacteria in marine systems. We herein describe the CAZymes of Paenibacillus algicola HB172198(T), a novel type species isolated from brown algae in Qishui Bay, Hainan, China. The genome of strain HB172198(T) is a 4,475,055 bp circular chromosome with an average GC content of 51.2%. Analysis of the nucleotide sequences of the predicted genes shows that strain HB172198(T) encodes 191 CAZymes. Abundant putative enzymes involved in the degradation of polysaccharides were identified, such as alginate lyase, agarase, carrageenase, xanthanase, xylanase, amylases, cellulase, chitinase, fucosidase and glucanase. Four of the putative polysaccharide lyases from families 7, 15 and 38 were involved in alginate degradation. The alginate lyases of strain HB172198(T) exhibited the maximum activity 152 U/mL at 50 °C and pH 8.0, and were relatively stable at pH 7.0 and temperatures lower than 40 °C. The average degree of polymerization (DP) of the sodium alginate oligosaccharide (AOS) degraded by the partially purified alginate lyases remained around 14.2, and the thin layer chromatography (TCL) analysis indicated that it contained DP2-DP8 oligosaccharides. The complete genome sequence of P. algicola HB172198(T) will enrich our knowledge of the mechanism of polysaccharide lyase production and provide insights into its potential applications in the degradation of polysaccharides such as alginate. MDPI 2022-06-09 /pmc/articles/PMC9227215/ /pubmed/35736191 http://dx.doi.org/10.3390/md20060388 Text en © 2022 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 Article
Huang, Huiqin
Zheng, Zhiguo
Zou, Xiaoxiao
Wang, Zixu
Gao, Rong
Zhu, Jun
Hu, Yonghua
Bao, Shixiang
Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
title Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
title_full Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
title_fullStr Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
title_full_unstemmed Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
title_short Genome Analysis of a Novel Polysaccharide-Degrading Bacterium Paenibacillus algicola and Determination of Alginate Lyases
title_sort genome analysis of a novel polysaccharide-degrading bacterium paenibacillus algicola and determination of alginate lyases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9227215/
https://www.ncbi.nlm.nih.gov/pubmed/35736191
http://dx.doi.org/10.3390/md20060388
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