Inhibition of dextransucrase activity in Streptococcus mutans by plant phenolics.

نویسندگان

  • Dimple Goyal
  • Sukesh Sharma
  • Akhtar Mahmood
چکیده

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 used chewing sticks (Acacia arabica, Azadirachta indica, Pongamia pinnata and Salvadora persica) for prevention of dental caries on hydrolytic activity of dextransucrsae in S. mutans. Gallic acid (4-5 mM) produced 80-90% inhibition of the enzyme, while tannic acid (0.2 mM) and syringic acid (5 mM) inhibited the enzyme activity 80% and 48%, respectively in vitro. The aqueous extracts of chewing sticks produced 35-40% inhibition of dextransucrase activity at 5 mg phenol concentration. Kinetic analysis revealed mixed-type of enzyme inhibition by polyphenols, where both K(m) and V(max) were altered. The value of K(i) for tannic, gallic and syringic acids were 0.35, 1.6 and 1.94 mM, respectively. The enzyme inhibition by polyphenols was optimum at pH 7-7.5, while by plant extract was maximum at pH 5-6. These results suggest that plant polyphenols may find potential applications in the prevention and control of dental caries by inhibiting dextransucrase activity in S. mutans.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Acceleration of dextransucrase activity of Streptococcus mutans by secretory immunoglobulin A.

The effect of immunoglobulins on the activity of dextransucrase purified from Streptococcus mutans strain HS-6 is described. When human salivary immunoglobulin A (IgA) or colostral IgA, either natured or denatured, was incubated with dextransucrase, the rate of the dextran synthesis was markedly accelerated, whereas human serum IgA or IgG neither accelerated nor inhibited the enzyme activity. T...

متن کامل

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...

متن کامل

Preferential utilization of the glucosyl moiety of sucrose by a cariogenic strain of Streptococcus mutans.

The utilization of sucrose by a cariogenic strain of Streptococcus mutans was studied. The soluble and cell-bound sucrose-dependent, polymer-forming sucrase activities constitutively produced by the bacteria during growth on glucose were measured. About eight times more dextransucrase activity was present than levan-sucrase activity. During various states of growth on sucrose, S. mutans accumul...

متن کامل

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...

متن کامل

Adherence of Streptococcus mutans to dextran synthesized in the presence of extracellular dextransucrase.

Live or heat-killed cells of Streptococcus mutans specifically adhere to dextran previously synthesized on glass surfaces by the action of extracellular dextransucrase.

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Indian journal of biochemistry & biophysics

دوره 50 1  شماره 

صفحات  -

تاریخ انتشار 2013