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Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque

The cold-adapted and/or salt-tolerant enzymes from marine microorganisms were confirmed to be meritorious tools to enhance the efficiency of biocatalysis in industrial biotechnology. We purified and characterized a dextranase CeDex from the marine bacterium Cellulosimicrobium sp. THN1. CeDex acted i...

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Autores principales: Xu, Linxiang, Zhang, Yan, Liu, Nannan, Wei, Zhen, Wang, Zhen, Wang, Yonghua, Wang, Shujun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9691899/
https://www.ncbi.nlm.nih.gov/pubmed/36439846
http://dx.doi.org/10.3389/fmicb.2022.1012957
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author Xu, Linxiang
Zhang, Yan
Liu, Nannan
Wei, Zhen
Wang, Zhen
Wang, Yonghua
Wang, Shujun
author_facet Xu, Linxiang
Zhang, Yan
Liu, Nannan
Wei, Zhen
Wang, Zhen
Wang, Yonghua
Wang, Shujun
author_sort Xu, Linxiang
collection PubMed
description The cold-adapted and/or salt-tolerant enzymes from marine microorganisms were confirmed to be meritorious tools to enhance the efficiency of biocatalysis in industrial biotechnology. We purified and characterized a dextranase CeDex from the marine bacterium Cellulosimicrobium sp. THN1. CeDex acted in alkaline pHs (7.5–8.5) and a broad temperature range (10–50°C) with sufficient pH stability and thermostability. Remarkably, CeDex retained approximately 40% of its maximal activities at 4°C and increased its activity to 150% in 4 M NaCl, displaying prominently cold adaptation and salt tolerance. Moreover, CeDex was greatly stimulated by Mg(2+), Na(+), Ba(2+), Ca(2+) and Sr(2+), and sugarcane juice always contains K(+), Ca(2+), Mg(2+) and Na(+), so CeDex will be suitable for removing dextran in the sugar industry. The main hydrolysate of CeDex was isomaltotriose, accompanied by isomaltotetraose, long-chain IOMs, and a small amount of isomaltose. The amino acid sequence of CeDex was identified from the THN1 genomic sequence by Nano LC–MS/MS and classified into the GH49 family. Notably, CeDex could prevent the formation of Streptococcus mutans biofilm and disassemble existing biofilms at 10 U/ml concentration and would have great potential to defeat biofilm-related dental caries.
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spelling pubmed-96918992022-11-26 Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque Xu, Linxiang Zhang, Yan Liu, Nannan Wei, Zhen Wang, Zhen Wang, Yonghua Wang, Shujun Front Microbiol Microbiology The cold-adapted and/or salt-tolerant enzymes from marine microorganisms were confirmed to be meritorious tools to enhance the efficiency of biocatalysis in industrial biotechnology. We purified and characterized a dextranase CeDex from the marine bacterium Cellulosimicrobium sp. THN1. CeDex acted in alkaline pHs (7.5–8.5) and a broad temperature range (10–50°C) with sufficient pH stability and thermostability. Remarkably, CeDex retained approximately 40% of its maximal activities at 4°C and increased its activity to 150% in 4 M NaCl, displaying prominently cold adaptation and salt tolerance. Moreover, CeDex was greatly stimulated by Mg(2+), Na(+), Ba(2+), Ca(2+) and Sr(2+), and sugarcane juice always contains K(+), Ca(2+), Mg(2+) and Na(+), so CeDex will be suitable for removing dextran in the sugar industry. The main hydrolysate of CeDex was isomaltotriose, accompanied by isomaltotetraose, long-chain IOMs, and a small amount of isomaltose. The amino acid sequence of CeDex was identified from the THN1 genomic sequence by Nano LC–MS/MS and classified into the GH49 family. Notably, CeDex could prevent the formation of Streptococcus mutans biofilm and disassemble existing biofilms at 10 U/ml concentration and would have great potential to defeat biofilm-related dental caries. Frontiers Media S.A. 2022-11-11 /pmc/articles/PMC9691899/ /pubmed/36439846 http://dx.doi.org/10.3389/fmicb.2022.1012957 Text en Copyright © 2022 Xu, Zhang, Liu, Wei, Wang, Wang and Wang. 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
Xu, Linxiang
Zhang, Yan
Liu, Nannan
Wei, Zhen
Wang, Zhen
Wang, Yonghua
Wang, Shujun
Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque
title Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque
title_full Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque
title_fullStr Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque
title_full_unstemmed Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque
title_short Purification and characterization of cold-adapted and salt-tolerant dextranase from Cellulosimicrobium sp. THN1 and its potential application for treatment of dental plaque
title_sort purification and characterization of cold-adapted and salt-tolerant dextranase from cellulosimicrobium sp. thn1 and its potential application for treatment of dental plaque
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9691899/
https://www.ncbi.nlm.nih.gov/pubmed/36439846
http://dx.doi.org/10.3389/fmicb.2022.1012957
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