Reduction of the adherence of Streptococcus sobrinus insoluble α-d-glucan by endo-(1→3)-α-d-glucanase

Inoue, Masakazu; Yakushiji, Tsuyoshi; Katsuki, Midori; Kudo, Naoko; Kinoshita, Toshihiko

doi:10.1016/0008-6215(88)84008-4

Cited by 22 publications

(12 citation statements)

References 20 publications

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“…a-1,3-glucanase exhibited a degrading activity against Streptococcal biofilms (Guggenheim and Haller, 1972;Imai et al, 1977;Inoue et al, 1988;Pleszczy¢ nska et al, 2010;Shimotsuura et al, 2008;Tsumori et al, 2011;Wiater et al, 2004Wiater et al, , 2005. However, the practical use of the enzyme still remains uncertain.…”

Section: Discussionmentioning

confidence: 99%

A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

Suyotha

Fujiki

Cherdvorapong

et al. 2017

J. Gen. Appl. Microbiol.

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Section: Discussionmentioning

confidence: 99%

A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

Suyotha

Fujiki

Cherdvorapong

et al. 2017

J. Gen. Appl. Microbiol.

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“…Results from numerous studies have shown that insoluble-glucan polymers play a major role in the development of dental plaque and the onset and progression of dental disease (for review, see [7] and references cited therein). Thus, strategies to reduce the disease potential of dental plaque have included the possibility of using carbohydrate-degrading enzymes to disrupt the molecular architecture of plaque [9][10][11]. One such enzyme, a(1 ~ 3) glucan, 3-glucanohydrolase (termed mutanase), from the filamentous fungus Trichoderma harzianum, has shown some potential as a caries preventative agent because it degrades the water-insoluble glucan present in dental plaque (referred to as mutan) [6,11].…”

Section: Introductionmentioning

confidence: 99%

Raffinose-induced mutanase production from Trichoderma harzianum

Quivey

1993

FEMS Microbiology Letters

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The enzyme alpha(1-->3),3-glucanohydrolase (referred to as mutanase) from the filamentous fungus Trichoderma harzianum OMZ 779 is capable of degrading the water-insoluble glucan in dental plaque. Previously, it was necessary to produce the glucan (referred to as mutan) in vitro for use as the sole carbon source and inducer of mutanase synthesis in fungal cultures. We report here that raffinose also induces the production of mutanase. The metabolism of raffinose differed from that of other sugars in metabolic end products and secreted protein profile. In addition to mutanase, we observed an approximately 15,000 M(r) protein that was also regulated by carbon source and by illumination conditions.

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“…Similarly, Inoue et al indicated that it took 24 h for the Pseudomonas sp. mutanase to dissociate insoluble glucan by cell-free GTFs (20). To our knowledge, there have been no reports which assessed the efficacy of mutanases when the biofilms were treated with enzymes for relatively short periods.…”

Section: Discussionmentioning

confidence: 99%

“…mutanase at 37°C for 90 min. Inoue et al (20) also reported that insoluble glucan formed by cell-free S. mutans OMZ 176 glucosyltransferases (GTFs) was degraded by incubation with Pseudomonas sp. mutanase at 37°C for 24 h. To our knowledge, however, little is known about mutanases having the ability to degrade biofilms following short-term treatments.…”

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confidence: 99%

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

Shimotsuura

Kigawa

Ohdera

et al. 2008

Appl Environ Microbiol

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A novel type of mutanase (termed mutanase RM1) was isolated from Paenibacillus sp. strain RM1. The purified enzyme specifically hydrolyzed ␣-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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Reduction of the adherence of Streptococcus sobrinus insoluble α-d-glucan by endo-(1→3)-α-d-glucanase

Cited by 22 publications

References 20 publications

A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

Raffinose-induced mutanase production from Trichoderma harzianum

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

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