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Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm

Laetiporus sulphureus is a source of α-1,3-glucan that can substitute for the commercially-unavailable streptococcal mutan used to induce microbial mutanases. The water-insoluble fraction of its fruiting bodies from 0.15 to 0.2% (w/v) induced mutanase activity in Paenibacillus sp. MP-1 at 0.35 μ ml(...

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Detalles Bibliográficos
Autores principales: Pleszczyńska, M., Wiater, A., Szczodrak, J.
Formato: Texto
Lenguaje:English
Publicado: Springer Netherlands 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2952102/
https://www.ncbi.nlm.nih.gov/pubmed/20623316
http://dx.doi.org/10.1007/s10529-010-0346-1
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author Pleszczyńska, M.
Wiater, A.
Szczodrak, J.
author_facet Pleszczyńska, M.
Wiater, A.
Szczodrak, J.
author_sort Pleszczyńska, M.
collection PubMed
description Laetiporus sulphureus is a source of α-1,3-glucan that can substitute for the commercially-unavailable streptococcal mutan used to induce microbial mutanases. The water-insoluble fraction of its fruiting bodies from 0.15 to 0.2% (w/v) induced mutanase activity in Paenibacillus sp. MP-1 at 0.35 μ ml(−1). The mutanase extensively hydrolyzed streptococcal mutan, giving 23% of saccharification, and 83% of solubilization of glucan after 6 h. It also degraded α-1,3-polymers of biofilms, formed in vitro by Streptococcus mutans, even after only 3 min of contact.
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spelling pubmed-29521022010-10-21 Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm Pleszczyńska, M. Wiater, A. Szczodrak, J. Biotechnol Lett Original Research Paper Laetiporus sulphureus is a source of α-1,3-glucan that can substitute for the commercially-unavailable streptococcal mutan used to induce microbial mutanases. The water-insoluble fraction of its fruiting bodies from 0.15 to 0.2% (w/v) induced mutanase activity in Paenibacillus sp. MP-1 at 0.35 μ ml(−1). The mutanase extensively hydrolyzed streptococcal mutan, giving 23% of saccharification, and 83% of solubilization of glucan after 6 h. It also degraded α-1,3-polymers of biofilms, formed in vitro by Streptococcus mutans, even after only 3 min of contact. Springer Netherlands 2010-07-11 2010 /pmc/articles/PMC2952102/ /pubmed/20623316 http://dx.doi.org/10.1007/s10529-010-0346-1 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Original Research Paper
Pleszczyńska, M.
Wiater, A.
Szczodrak, J.
Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm
title Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm
title_full Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm
title_fullStr Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm
title_full_unstemmed Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm
title_short Mutanase from Paenibacillus sp. MP-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and Streptococcus mutans biofilm
title_sort mutanase from paenibacillus sp. mp-1 produced inductively by fungal α-1,3-glucan and its potential for the degradation of mutan and streptococcus mutans biofilm
topic Original Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2952102/
https://www.ncbi.nlm.nih.gov/pubmed/20623316
http://dx.doi.org/10.1007/s10529-010-0346-1
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