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Journal of Dental Research, Vol 55, 886-892, Copyright © 1976 by International & American Associations for Dental Research Online Journals


ARTICLES

Comparison of dextranases for their possible use in eliminating dental plaque

B. Goldstein-Lifschitz and S. Bauer

Dextranases produced by P lilacinum NRRL 896 and NRRL 895 and by P funiculosum NRRL 1768 were studied for their possible incorporation into a dental plaque elimination system. The following properties of the enzymes were compared: effect of the pH level on the activity and the stability of the enzymes on the acid side of the pH range; molecular weight; affinity to Sephadex G-25 which served as a model for insoluble dextran in plaques; and the extent of hydrolytic action on dextrans containing alpha-1,3, alpha-1,4 and alpha-1,6 bonds in various proportions. The enzyme of P funiculosum NRRL 1768 certainly has its limitations as a plaque-degrading enzyme, for example, diminished activity at a high pH level and lack of activity on alpha-1,3 bonds. However, from our studies, and from a survey of the relevant literature with respect to the aforementioned properties in other dextranases, the enzyme of P funiculosum NRRL 1768 emerges as a suitable choice for incorporation as dextranase, possibly together with other enzymes, into an enzymatic dental plaque elimination system.


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Microbiol. Mol. Biol. Rev.Home page
E. Khalikova, P. Susi, and T. Korpela
Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications
Microbiol. Mol. Biol. Rev., June 1, 2005; 69(2): 306 - 325.
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