Background/purpose The co-operative effect of exogenous dextranase (Dex) and sodium fluoride (NaF) on Streptococcus mutans monospecies biofilms is impressive. Here we investigated the effects of the combination on a mature cariogenic multispecies biofilm and analyzed the potential mechanism. Materials and methods A multispecies biofilm of S. mutans , Lactobacillus acidophilus , and Actinomyces viscosus was established in vitro . Dex and NaF were added separately or together. The effects of the agents on the biomass were measured. The exopolysaccharide production was determined with the scintillation counting method. The viability and morphology were evaluated using colony forming unit and confocal laser scanning microscopy, respectively. Results In general, biofilms treated with Dex and a little concentration of NaF exhibited a lower biomass, exopolysaccharide production, and viability compared with the control group (P < 0.05). Confocal laser scanning microscopy using a vital fluorescence technique showed the combination treated biofilms appeared to be loose relatively and single cells could be observed. Furthermore, the thickness and viability were also lower than either of the separate agent groups (P < 0.05). Conclusion Overall, these findings reveal that a combination of 1 U/mL Dex and 80 μg/mL NaF is a promising candidate for disrupting complex cariogenic multispecies biofilms. This feature may be in that Dex loses the structure of biofilms, thereby facilitating NaF penetration and enhancing its antibacterial effects.

Tannases, mainly produced by microorganisms, are able to hydrolyze gallotannins, ellagitannins, complex tannins, and gallic acid esters into gallic acid, ellagic acid, glucose, or alcohols, and also synthesize gallic acid esters using tannic acid or gallic acid with a variety of alcohols in nonaqueous media. Microbial tannases have been widely applied especially in beverage processing, pharmaceutics, and brewing. However, many factors, especially high production costs, severely limit the use of microbial tannases at the industrial level. In this minireview, we aim to provide an overview of the advances in applications of microbial tannases during the last 15 years, mainly including the following respects: hydrolysis of tea cream, modification of green tea catechins, production of gallic acid, debittering of fruit juices, degradation of tannery effluents, and synthesis of propyl gallate, trying to know the trends and prospects for the future in applications of microbial tannases.

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VicRK (WalRK or YycFG) is a conserved 2-component regulatory system (TCS) that regulates cell division, cell wall biosynthesis, and homeostasis in low-GC Gram-positive bacteria. VicRK is also associated with biofilm formation of Streptococcus mutans on the tooth surface as it directly regulates the extracellular polysaccharide (EPS) synthesis. Of the 2 components, VicK possesses both autokinase and phosphatase activities, which regulate the phosphorylation and dephosphorylation of the regulator VicR in response to environmental cues. However, the dual mechanism of VicK as the autokinase/phosphatase in regulating S. mutans’ responses is not well elucidated. Previously, it has been shown that the phosphatase activity depends on the PAS domain and residues in the DHp domain of VicK in S. mutans. Specifically, mutating proline at 222 in the PAS domain inhibits VicK phosphatase activity. We generated a VicKP222A mutant to determine the level of VicR-P in the cytoplasm by Phos-tag sodium dodecyl sulfate polyacrylamide gel electrophoresis. We show that in VicKP222A phosphatase, attenuation increased phosphorylated VicR (VicR-P) that downregulated glucosyltransferases, gtfBC, thereby reducing the synthesis of water-insoluble polysaccharides (WIS-EPS) in the biofilm. In addition, VicKP222A presented as long-rod cells, reduced growth, and displayed asymmetrical division. A major adhesin of S. mutans, SpaP was downregulated in VicKP222A, making it unable to agglutinate in saliva. In summary, we have confirmed that VicK phosphatase activity is critical to maintain optimal phosphorylation status of VicR in S. mutans, which is important for cell growth, cell division, EPS synthesis, and bacterial agglutination in saliva. Hence, VicK phosphatase activity may represent a promising target to modulate S. mutans’ pathogenicity.