A comparative study of extracellular glucanhydrolase and glucosyltransferase enzyme activities of five different serotypes of oral Streptococcus mutans

Felgenhauer, Bruce E.; Trautner, K

doi:10.1016/0003-9969(82)90084-x

Cited by 5 publications

(7 citation statements)

References 27 publications

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“…The size of the protein observed in culture supernatant (180 kDa) in our study was divergent with the previous report that the dextranase extracted from the culture supernatant of S. criceti E49 was observed at about 116 kDa (17), suggesting the divergence of sample preparation. It was reported that the dextranase activity of S. criceti was weakest in mutans streptococci (serotypes a, b, c, d, and e) whereas the dextranase activity of S. sobrinus serotype d was 39 times stronger than that of S. criceti (6). This weak activity of extracellular dextranase in S. criceti might account for the small amount of dextranase protein in the culture supernatant and low level of promoter activity of the dex gene.…”

Section: Discussionmentioning

confidence: 98%

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Identification and Characterization of a Dextranase Gene of Streptococcus criceti

Tamura

Yamada

Kato

2007

Microbiology and Immunology

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The dextranase gene, dex, was identified in Streptococcus criceti strain E49 by degenerate PCR and sequenced completely by the gene‐walking method. A sequence of 3,960 nucleotides was determined. The dex gene encodes a 1,200‐amino acid protein, which has a calculated molecular mass of 128,129.91 and pI of 4.15 and is predicted to be a cell‐surface protein. The deduced amino acid sequence of dex showed homology to S. downei dextranase (63.9% identity). Phylogenetic analysis revealed the similarity of the deduced amino acid sequence of dextranases in S. criceti, S. sobrinus, and S. downei. A recombinant form of the protein with six histidine residues tagged in the C‐terminus was partially purified and showed dextranase activity on blue‐dextran sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (BD‐SDS‐PAGE) followed by renaturation. We also detected dextranase activity in S. criceti cell extracts and culture supernatant by renatured BD‐SDS‐PAGE, whereas no dextranase activity of the cells was observed on blue‐dextran brain heart infusion (BD‐BHI) agar plates. Furthermore, PCR‐based mutations of dextranase indicated that a deletion mutant of the C‐terminal region could hydrolyze blue dextrans and that the D453E mutation, W793L mutation, and double mutations (W793L and deletion of the C‐terminal region) resulted in a loss of dextranase activity. These findings suggest that Asp‐453 and Trp‐793 residues of S. criceti dextranase are critical to the enzyme's activity.

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Section: Discussionmentioning

confidence: 98%

“…In contrast, dextranase activity was preserved at a low level in the culture supernatant of S. criceti (6). Thereafter, the dextranase gene was detected in S. criceti E49 by dot blot hybridization analysis (17) and the 525-bp nucleotide sequence of the dextranase gene of S. criceti ATCC19642 (HS-6) was determined (12).…”

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confidence: 99%

Identification and Characterization of a Dextranase Gene of Streptococcus criceti

Tamura

Yamada

Kato

2007

Microbiology and Immunology

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“…They are believed to be responsible for the formation of dental plaque and the induction of caries on the surface of teeth and have, therefore, been a subject of numerous studies (11,23,46,55). The glucanproducing streptococci S. sanguis, S. bovis, and S. mutans are also the most frequent organisms associated with endocarditis in humans.…”

Section: Role Of Dextranases In Dextran-producing Microorganismsmentioning

confidence: 99%

“…Oral streptococci are predominant producers of the dextranases (24,46,55,220). Strains of S. mutans constitutively produce both endo-and exodextranases (162,171,220), whereas S. sobrinus synthesizes only endodextranase (10,222).…”

Section: Role Of Dextranases In Dextran-producing Microorganismsmentioning

confidence: 99%

“…Endodextranase activity is present in the culture filtrates, while dextran glucosidase is predominantly cell associated (220). Endodextranase may regulate glucan synthesis by altering the ratio of ␣-1,6 to ␣-1,3 linkages and modify the glucan substrate to a firmer form, hence influencing its solubility and adhesive properties (25,46,220). Therefore, dextranase activity influences sucrosedependent adherence of bacterial cells.…”

Section: Role Of Dextranases In Dextran-producing Microorganismsmentioning

confidence: 99%

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Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Khalikova

Susi

Korpela

2005

Microbiol Mol Biol Rev

228

152

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Dextran is a chemically and physically complex polymer, breakdown of which is carried out by a variety of endo- and exodextranases. Enzymes in many groups can be classified as dextranases according to function: such enzymes include dextranhydrolases, glucodextranases, exoisomaltohydrolases, exoisomaltotriohydrases, and branched-dextran exo-1,2-α-glucosidases. Cycloisomalto-oligosaccharide glucanotransferase does not formally belong to the dextranases even though its side reaction produces hydrolyzed dextrans. A new classification system for glycosylhydrolases and glycosyltransferases, which is based on amino acid sequence similarities, divides the dextranases into five families. However, this classification is still incomplete since sequence information is missing for many of the enzymes that have been biochemically characterized as dextranases. Dextran-degrading enzymes have been isolated from a wide range of microorganisms. The major characteristics of these enzymes, the methods for analyzing their activities and biological roles, analysis of primary sequence data, and three-dimensional structures of dextranases have been dealt with in this review. Dextranases are promising for future use in various scientific and biotechnological applications

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Stufenweises Prüfschema für Zuckeraustauschstoffe — Vorprüfung mittels Enzymen 4. Glucosyltransferasen ausStreptococcus mutans AHT

Forsthuber

Siebert

1988

Z Ernährungswiss

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A continuous procedure for the simultaneous enzymatic measurement of the release of free fructose and glucose was adapted to the kinetic conditions of the synthesis of polysaccharides from sucrose by glucosyltransferases from Streptococcus mutans AHT. Initial velocities, Km of sucrose, and the efficiency of the formation of glucans from sucrose can be determined. Longtime incubations with the isolation of soluble and insoluble glucans as an established method were compared with the new procedure. As examples of the effect of sugar substitutes on glucosyltransferases, data on leucrose, nystose, Palatinit, xylitol, leucritol and polyglucose PL-3 are presented. The results provide a preliminary assessment of sugar substitutes such as non-cariogenic sweeteners.

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A comparative study of extracellular glucanhydrolase and glucosyltransferase enzyme activities of five different serotypes of oral Streptococcus mutans

Cited by 5 publications

References 27 publications

Identification and Characterization of a Dextranase Gene of Streptococcus criceti

Identification and Characterization of a Dextranase Gene of Streptococcus criceti

Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Stufenweises Prüfschema für Zuckeraustauschstoffe — Vorprüfung mittels Enzymen 4. Glucosyltransferasen ausStreptococcus mutans AHT

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