About: Dextranase is a research topic. Over the lifetime, 692 publications have been published within this topic receiving 10780 citations. The topic is also known as: dextran hydrolase & 1,6-alpha-D-glucan 6-glucanohydrolase.
TL;DR: A new method utilizing an enzyme digestible immunoabsorbent has permitted fractionation and purification of lymphoid cells according to their surface properties and ninety-eight per cent of the absorbed B cells could be recovered in a functionally viable state after solubilization of the immunoAbsorbent with dextranase.
Abstract: Summary A new method utilizing an enzyme digestible immunoabsorbent has permitted fractionation and purification of lymphoid cells according to their surface properties. Spleen cells filtered through Sephadex anti-Fab columns were specifically depleted of immunoglobulin-bearing B cells. Passed cells, on the other hand, were enriched both in T and null staining cells. Ninety-eight per cent of the absorbed B cells could be recovered in a functionally viable state after solubilization of the immunoabsorbent with dextranase.
TL;DR: The production of dextransucrase from Leuconostoc mesenteroides NRRL B-512F was stimulated 2-fold by the addition of 0.005% of calcium chloride to the medium; levansucrase levels were unaffected; and the mannoglycoprotein character of the enzyme was confirmed.
TL;DR: It was shown by FTIR analysis that by a proper selection of the polymerization conditions, hydrogels could be obtained in which more than 95% of the methacrylate groups had reacted within 20 min and was dependent on the amount of dextranase in the gel.
TL;DR: The mechanism of adsorption of the Streptococcus mutans enzymes responsible for the synthesis of insoluble dextran-levan to the S. mutans cell-wall binding sites has been studied and these data present a partial explanation of the processes which may be concerned in the formation of dental plaque on the smooth surfaces of teeth.
Abstract: The mechanism of adsorption of the Streptococcus mutans enzymes responsible for the synthesis of insoluble dextran-levan to the S. mutans cell-wall binding sites has been studied. Certain characteristics of these binding sites are presented. The adsorption of these enzymes to the cell surface occurred rapidly without the addition of a source of energy and over a pH range of 3 to 11. The adsorption was inhibited by soluble dextran, probably due to the strong affinity of the polymer to the enzyme. All other polymers and sugars studied showed little or no inhibition. The adsorption was also inhibited by antibody globulin to the a-d immunologically specific group antigen surface polysaccharide of S. mutans and by anti-dextran globulin. The inhibition by anti-a-d globulin is considered to be due to a restriction of access of enzyme to the binding site of the enzyme which may be located in close proximity to the group antigen. On the other hand, anti-dextran globulin appeared to directly inhibit the adsorption by covering the binding site. Dextranase destroyed the binding site and released glucose from the S. mutans cells. These data indicate that S. mutans grown in media containing glucose possesses a small amount of dextran on the cell surface, and that this dextran is, or is a part of, the binding site for enzymes which synthesize the insoluble dextran-levan polymer. Trypsin inhibited the synthesis of insoluble polysaccharide and the adherence of cells. It is not clear in this case that destruction of the binding sites occurred. These data present a partial explanation of the processes which may be concerned in the formation of dental plaque on the smooth surfaces of teeth.