Interactions of dextransucrase purified from Streptococcus mutans 890 with plant polyphenols

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Inhibition of dextransucrase activity in Streptococcus mutans by plant phenolics.

Streptococcus mutans is responsible for causing dental caries in humans and utilizes sucrose for its growth. The dextransucrase (EC 2.4.1.5) is responsible for sucrose metabolism, which exhibits both hydrolytic and glucosyltransferase activities. In this study, we examined the effects of the plant phenols, namely gallic, tannic and syringic acids and aqueous extracts of certain traditionally us...

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Streptococcus mutans dextransucrase: requirement for primer dextran.

Dextran stimulation (priming) of the dextransucrase (EC 2.4.1.5) from Streptococcus mutans strain 6715 was studied. The dextransucrase activity in supernatant fluids from glucose-grown cultures was shown to be partially primer dependent. During extended storage at 4 C the enzyme retained its activity. However, the ability to make dextran became increasingly primer dependent. Hydroxylapatite-chr...

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Some Immunochemical Properties of Dextransucrase and Invertase from Streptococcus mutans.

Dextransucrase and invertase of some strains of Streptococcus mutans were examined by immunodiffusion with antisera against enzymes purified from strain HS-6 (Bratthall's serotype a). Both antisera cross-reacted with crude enzyme preparations from the other serotype a (strains HS-1 and AHT) and d organisms (strains KIR, OMZ176, and OMZ65) but not with those from serotype b (strains FA-1 and BHT...

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Purification and properties of dextransucrase from Streptococcus mutans.

The dextransucrase (EC 2.4.1.5) activity from cell-free culture supernatants of Streptococcus mutans strain 6715 has been purified approximately 1,500-fold by ammonium sulfate precipitation, hydroxylapatite chromatography, and isoelectric focusing. The enzyme was eluted as a single peak of activity from hydroxylapatite, and isoelectric focusing of the resulting preparation gave a single band of...

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Specific method for the purification of Streptococcus mutans dextransucrase.

A convenient and rapid method for the purification of Streptococcus mutans dextransucrase is described. Affinity chromatography, on a column containing insoluble dextran purified from a culture of S. mutans 6715-49, gave an almost 300-fold purification, with 76% recovery of enzyme. Subsequent hydrophobic chromatography on butyl-agarose increased the overall enzyme purification to more than 1,00...

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ژورنال

عنوان ژورنال: Biochemistry and Biophysics Reports

سال: 2021

ISSN: 2405-5808

DOI: 10.1016/j.bbrep.2021.100980