ArticleApplied and environmental microbiology2008
Biochemical and molecular characterization of a novel type of Mutanase from Paenibacillus sp. strain RM1: identification of its mutan-binding domain, essential for degradation of Streptococcus mutans biofilms.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 36 citations in OpenAlex.
- Enzymatic tools for the treatment of caries-associated biofilms: Investigating the enzymes of a putative polysaccharide utilization locus from Prevotella melaninogenica and their application against Streptococcus mutans biofilm.World journal of microbiology & biotechnology · 2026Article
- Structural and biochemical basis for activity of Aspergillus nidulans α-1,3-glucanases from glycoside hydrolase family 71.Communications biology · 2025Article
- Effect of mutanase and dextranase on biofilms of cariogenic bacteria: A systematic review ofBiofilm · 2024Review
- α-1,3-Glucanase from the gram-negative bacterium Flavobacterium sp. EK-14 hydrolyzes fungal cell wall α-1,3-glucan.Scientific reports · 2023Article
- Recombinant Prevotella melaninogenica α-1,3 glucanase and Capnocytophaga ochracea α-1,6 glucanase as enzymatic tools for in vitro degradation of S. mutans biofilms.World journal of microbiology & biotechnology · 2023Article
- Crystal structure of the catalytic unit of GH 87-type α-1,3-glucanase Agl-KA from Bacillus circulans.Scientific reports · 2019Article
- X-ray crystallographic analysis of the catalytic domain of α-1,3-glucanase FH1 from Paenibacillus glycanilyticus overexpressed in Brevibacillus choshinensis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Penetration of an antimicrobial zinc-sugar alcohol complex into Streptococcus mutans biofilms.Scientific reports · 2018Article
- Spontaneous detachment of Streptococcus mutans biofilm by synergistic effect between zwitterion and sugar alcohol.Scientific reports · 2017Article
- α-1,3-Glucanase: present situation and prospect of research.World journal of microbiology & biotechnology · 2016Review
- 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.Biotechnology letters · 2010Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A novel type of mutanase (termed mutanase RM1) was isolated from Paenibacillus sp. strain RM1. The purified enzyme specifically hydrolyzed alpha-1,3-glucan (mutan) and effectively degraded biofilms formed by Streptococcus mutans, a major etiologic agent in the progression of dental caries, even following brief incubation. The nucleotide sequence of the gene for this protein contains a 3,873-bp open reading frame encoding 1,291 amino acids with a calculated molecular mass of 135 kDa. The protein contains two major domains, the N-terminal domain (277 residues) and the C-terminal domain (937 residues), separated by a characteristic sequence composed of proline and threonine repeats. The characterization of the recombinant proteins for each domain which were expressed in Escherichia coli demonstrated that the N-terminal domain had strong mutan-binding activity but no mutanase activity whereas the C-terminal domain was responsible for mutanase activity but had mutan-binding activity significantly lower than that of the intact protein. Importantly, the biofilm-degrading activity observed with the intact protein was not exhibited by either domain alone or in combination with the other. Therefore, these results indicate that the structural integrity of mutanase RM1 containing the N-terminal mutan-binding domain is required for the biofilm-degrading activity.
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