Hydrolysis of mutan and prevention of its formation in streptococcal films by fungal α-d-glucanases

Wiater, Adrian; Szczodrak, Janusz; Rogalski, Jerzy

doi:10.1016/s0032-9592(03)00281-4

Cited by 32 publications

(56 citation statements)

References 29 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%

“…Thus, the enzyme is of interest due to its potential use in the removal of dental plaque and the biological control of pathogenic fungi. Some studies have demonstrated the ability of a-1,3-glucanases to reduce the plaque synthesized by Streptococcus species, as well as to inhibit plaque formation (Fuglsang et al, 2000;Pleszczy¢ nska et al, 2010;Shimotsuura et al, 2008;Tsumori et al, 2011;Wiater et al, 2004Wiater et al, , 2008. Moreover, they indicated that the degradation of plaque by the enzyme was more effectively performed in combination with dextranase (Fuglsang et al, 2000;Shimotsuura et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

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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“…It is likely that similar findings were observed wherein α-glucanase from Trichoderma harzianum cleaved α-1,3-linkages in some insolu- ble glucans of streptococci. 10,11) Thus, the present mutanase from fermented food should be able to hydrolyze and solubilize glucans in biofilms formed by cariogenic streptococci in vivo. 12) …”

Section: Mutanase Hydrolyzed Insoluble Glucans Which Were Synthesizementioning

confidence: 99%

Substrate Specificity of Mutanase of Paenibacillus humicus from Fermented Food

Tsumori

Shimamura

Sakurai

et al. 2011

JOURNAL OF HEALTH SCIENCE

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Mutanase, α-1,3-glucanase, catalyzes the hydrolysis of α-1,3-glucans, and is expected for preventive medicine, since the enzyme has an ability for hydrolysis of insoluble glucans that are synthesized by cariogenic streptococci. We previously isolated the mutanase of Paenibacillus humicus from fermented soybeans. In the present study, Paenibacillus mutanase was characterized with respect to its hydrolysis efficiency of insoluble glucans, and mode of action on α-1,3-glucan oligosaccharides. Recombinant mutanase hydrolyzed insoluble glucans of cariogenic streptococci efficiently. Enzymatic reaction on hydrolysis of mutan, we assumed that the enzyme cleaved the substrate in an endo-catalytic manner. The hydrolysis of α-1,3-glucan oligosaccharides gave α-1,3-glucan tetrasaccharide as the primary final product but α-1,3-glucan pentasaccharide was the minimal size of substrate on which the enzyme catalyzed. Mutanase hydrolyzed borohydride-treated α-1,3-glucan hexasaccharide into the tetrasaccharide and the disaccharide-alditol. Thus, the enzyme cleaved the fourth α-1,3-glucosidic linkage from the non-reducing end of the oligosaccharides. Mutanase in fermented food should be capable of removing streptococcal insoluble glucans that can induce dental caries.

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“…2) This adhesion is mediated by insoluble glucan biofilms, the components of which are synthesized by a series of glucosyltransferases from cariogenic streptococci. 3) Thus, formation of dental plaque leads to dental caries. The enzymatic glycolysis of mutan expects to liberate the biofilm from tooth surface and prevent dental caries.…”

Section: Introductionmentioning

confidence: 99%

Mutanase of Paenibacillus humicus from Fermented Food Has a Potential for Hydrolysis of Biofilms Synthesized by Streptococcus mutans

Tsumori

Shimamura

Sakurai

et al. 2011

JOURNAL OF HEALTH SCIENCE

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Mutanase is an α-1,3-glucanase that cleaves the α-1,3-glucosidic linkages of glucan polysaccharides termed mutan. There has been interest in mutanase as it has the potential to be considered in preventive medicine. Previously, we identified the mutanase of Paenibacillus humicus from fermented soybeans and observed that the enzyme hydrolyzed insoluble glucans and mutan in vitro. Here we focused on the ability of mutanase in preventing dental caries. We proposed that the enzyme participates in the degradation of insoluble glucan biofilms in microplates, which were used as a model of biofilms on tooth surface. In this study, we investigated the potential of mutanase to hydrolyze insoluble glucan biofilms synthesized by a typical cariogenic streptococcus, Streptococcus mutans 10449, in 96-well microplates. The mutanase specifically hydrolyzed insoluble glucan biofilms composed of insoluble glucans synthesized by S. mutans. The mutanase hydrolyzed approximately 60% of S. mutans glucan biofilms in the wells and liberated oligosaccharides from the glucan films. We observed that recombinant mutanase could hydrolyze mutan biofilms, and the enzyme was characterized as an endo-α-1,3-glucanase because its hydrolysis of mutan biofilms, resulted in the predominant liberation of α-1,3-glucan tetrasaccharides. The present study suggests that Paenibacillus mutanase from fermented soybeans has potential application in preventive medicine because of its ability to degrade oral insoluble glucan biofilms.

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Hydrolysis of mutan and prevention of its formation in streptococcal films by fungal α-d-glucanases

Cited by 32 publications

References 29 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

Substrate Specificity of Mutanase of Paenibacillus humicus from Fermented Food

Mutanase of Paenibacillus humicus from Fermented Food Has a Potential for Hydrolysis of Biofilms Synthesized by Streptococcus mutans

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