Comparative Study of Invertases of
            <i>Streptococcus mutans</i>

Tanzer, Jason M.; Brown, Albert T.; McInerney, Marcia F.; Woodiel, Florence N.

doi:10.1128/iai.16.1.318-327.1977

Cited by 28 publications

(13 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…KusAMiTZu (11) found that the cariogenic Streptococcus mutans GS-5 possessed Pfructosidase activity, because partially purified enzymes (both extracellular and intracellular) hydrolyzed p-fructosides, but not a series of agiucosides. Similar observations were made by CHASSY et al (4) witb extracellular invertases from seven known oral streptococci (including five S. mutans strains), and by TANZER et al (21) with intracellular invertases isolated from the five Brathall serotypes of S. mutans. These studies mentioned that no splitting of maltose from tbe oral streptococci strains was obsei-ved by the enzyme extract.…”

Section: Discussionsupporting

confidence: 81%

“…Previous investigations (4,11,21) have claimed that the invertases in dental piaque are a-glucosidases or p-fructosidases, p-fructosidases being the m:ore important. It appears possible by the use of acarbose to obtain further information about this subject, Therefore, the aim ofthe present investigation was to examine the effect of acarbose (BAY g 5421) on the disaccharide splitting enzymes in the dentaf plaque and to determine the type of invertases present in the plaque.…”

mentioning

confidence: 95%

See 1 more Smart Citation

Effect of the α‐glucosidase inhibitor, acarbose, on disaccharide splitting enzymes in human dental plaque

Fiehn¹,

Moe²

1982

European J Oral Sciences

View full text Add to dashboard Cite

Effeel ofthe a-glucosidase inhibitor, acarhose, on disaccharide sphtting enzymes in human denta] plaque. Scand. J. Dent. Res. 1982: 90: 124-130. Abstract -Inhibition of microbial enzymes in human dental plaqtie catalyzing the cleavage of the disaccharides maltose, sucrose and lactose was carried out with the a-glucosidase inhibitor, acarbose. The maltases from piaque homogenates were totally inhibited, whereas the inhibition ofthe iBvertases varied considerably. With increasing inhibitor conceotrations, from 1 mM to 50 mM, the inhibition of the invertases increased. Preincubation Ibr 30 min ofthe plaque homogenate with inhibitor resulted in a 20% increase ofthe inhibition of invertase activity. The inhibitor showed non-competitive inhibition of the invertases in the homogenates, whereas tbe maltases were competitively inhibited. The lactases were not inhibited at all. The invertases from human dental plaque may be oi-glucosidases and/or P-fructosidases.

show abstract

Section: Discussionsupporting

confidence: 81%

mentioning

confidence: 95%

Effect of the α‐glucosidase inhibitor, acarbose, on disaccharide splitting enzymes in human dental plaque

Fiehn¹,

Moe²

1982

European J Oral Sciences

View full text Add to dashboard Cite

show abstract

“…Homogenate concentration was 10 mg/ml acetate buffer. 28,30,31). The present investigation with plaque homogenate has shown the apparent pH optimum of pH 5.9 for the invertases to be lower than that for the glycosyltransferases.…”

Section: Discussionmentioning

confidence: 47%

“…The presence in the sample of saliva, blood and dental calculus can easily result in an erroneous quautitation of the invertase activity. Furthermore inorganic phosphate from the calculus may have a strong positive effect on the invertases (31).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Method for determination of invertase acitivity in homogentes of human dental plaque

Fiehn

Moe

1981

European J Oral Sciences

View full text Add to dashboard Cite

– Supragingival human dental plaque was ecllected from patients with evidence of caries. The plaque was frozen and stored at‐20°C. Pooled plaque was homogenized in acelate buffer pH 5.0 in an ice‐water bath. By incubating the homogenate at pH 5.0 with [U‐°C]‐sucrose the formation fo glucose and fructose was followed. Incubation in acetate buffer at pH 5.0 eliminated the glycosyltransferase activities adn teh glycolytic pathway. Normal Michaclis‐Menten kinetics were observed until about 40 mM sucrose. At highert concentration of sucrose, excess substrate inhibition occurred. Storage of the homogenate at −20° C resulted in decrease of the invertase activity with time.

show abstract

Electrophoretic studies of extracellular glucosyltransferases and fructosyltransferases from seventeen strains of Streptococcus mutans

et al. 1987

View full text Add to dashboard Cite

Streptococcus mutans was classified by the electrophoretic properties of glucosyltransferases (GTases) and fructosyltransferases (FTases). The cells of serotypes a, d and g did not release extracellular FTases, although those from other serotypes did. The enzymes from cells of serotypes d and g synthesized a good deal of insoluble polysaccharide compared with other serotypes. The enzymes were applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and polyacrylamide gel-isoelectric focussing (PAG-IEF). Gels were stained for their activity and protein content. Enzymes belonging to the same serotype gave the same specific pattern on both gels. The seven serotypes could be classified into the following four groups: serotypes d and g, serotype a, serotypes c, e and f, and serotype b. The results agree well with some previous reports based on other methods. The molecular weights of three GTase bands were 156K, 146K and 135K, and of four kinds of FTase bands were 108K, 95K, 80K and 76K. The isoelectric points of main enzymes were 4.25, 4.60, 5.00, 5.55 and 5.70. Those of FTases were 4.25 and 4.60.

show abstract

Comparative Study of Invertases of Streptococcus mutans

Cited by 28 publications

References 32 publications

Effect of the α‐glucosidase inhibitor, acarbose, on disaccharide splitting enzymes in human dental plaque

Effect of the α‐glucosidase inhibitor, acarbose, on disaccharide splitting enzymes in human dental plaque

Method for determination of invertase acitivity in homogentes of human dental plaque

Electrophoretic studies of extracellular glucosyltransferases and fructosyltransferases from seventeen strains of Streptococcus mutans

Contact Info

Product

Resources

About