Reduction of the adherence of Streptococcus sobrinus insoluble α-d-glucan by endo-(1→3)-α-d-glucanase

✍ Scribed by Masakazu Inoue; Tsuyoshi Yakushiji; Midori Katsuki; Naoko Kudo; Toshihiko Koga

• Publisher: Elsevier Science
• Year: 1988
• Tongue: English
• Weight: 709 KB
• Volume: 182
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(88)84008-4

✦ Synopsis

Insoluble cu-o-glucan, previously formed on a glass surface from sucrose by the action of cell-free D-glucosyltransferases of Streptococcus sobrinus OMZl76, was significantly removed by a purified preparation of endo-(1+3)-cr-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 (l-6)-cu-o-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).