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• W2019909592 abstract "Insoluble α-d-glucan, previously formed on a glass surface from sucrose by the action of cell-free d-glucosyltransferases of Streptococcus sobrinus OMZ176, was significantly removed by a purified preparation of endo-(1→3)-α-d-glucanase (mutanase) from a strain of Pseudomonas sp. Almost complete dissociation of adherent glucan occurred at the highest enzyme concentration (40 mU/mL) tested. Synthesis and de novo adherence on glass of the glucan was markedly inhibited by the presence of mutanase, even at low concentrations (4 mU/mL or less). When compared to native glucan, the mutanase-modified glucan samples (a) contained lower proportion of d-(1→3) linkages; (b) showed lower susceptibility to mutanase and higher susceptibility to (1→6)-α-d-glucanase (dextranase); (c) contained larger amounts of low-molecular-weight fractions; (d) had lower intrinsic viscosities; (e) showed higher S. sobrinus cell-agglutinating activities; and (f) consisted of looser entwinement of coalescent single-stranded fibrils (a major component) and shorter double-stranded fibrils (a minor one)." @default.
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• W2019909592 date "1988-11-01" @default.
• W2019909592 modified "2023-10-02" @default.
• W2019909592 title "Reduction of the adherence of Streptococcus sobrinus insoluble α-d-glucan by endo-(1→3)-α-d-glucanase" @default.
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• W2019909592 doi "https://doi.org/10.1016/0008-6215(88)84008-4" @default.
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