Purification and Partial Characterization of a Novel Glucanhydrolase from<i>Lipomyces starkeyi</i>KSM 22 and its Use for Inhibition of Insoluble Glucan Formation

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  • Su-Jin RYU
    Department of Biochemical Engineering, Chonnam National University Department of Chemical Engineering, Chonnam National University
  • KIM Doman
    Department of Biochemical Engineering, Chonnam National University Research Institute for Catalysis, Chonnam National University Research Center for New-Biomaterials in Agriculture, Seoul National University
  • RYU Hwa-Ja
    Department of Biochemical Engineering, Chonnam National University Department of Fine Chemical Engineering, Chonnam National University
  • CHIBA Seiya
    Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
  • KIMURA Atsuo
    Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
  • DAY Donal F.
    The Audubon Sugar Instistute, Louisiana State University

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  • Purification and Partial Characterization of a Novel Glucanhydrolase from Lipomyces starkeyi KSM 22 and its Use for Inhibition of Insoluble Glucan Formation.

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  A novel glucanhydrolase from a mutant of Lipomyces starkeyi ATCC 74054 was purified. The single protein (100 kDa) showed either dextranolytic or amylolytic activity. We referred to the glucanhydrolase as a DXAMase. The DXAMase was produced in a starch medium and it was 3.75-fold more active for hydrolysis of the purified insoluble-glucan of Streptococcus mutans than Penicillium funiculosum dextranase. Aggregation of S. mutans cells with dextran and adherence to glass were eliminated by incubating with the DXAMase. The addition of DXAMase (0.1 IU/ml) to the mutansucrase reaction digest with sucrose reduced the formation of insoluble-glucan about 80%. Also the DXAMase (0.5 IU/ml) removed 80% of the pre-formed sucrose-dependent adherent film. These in vitro properties of L. starkeyi KSM 22 DXAMase are desirable for its application as a dental plaque control agent.<br>

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