| 摘要 |
NEW MATERIAL:Alkali pullulanase Z-1. Action: decomposes alpha-1,6-glucoside bonding of pullulan and forms maltotriose, then hydrolyzes bonding of starch, etc.; Substrate specificity: hydrolyzes the branch structure having a degree of polymerization larger than maltose among saccharides having a branch structure with branched bonding; Reactional pH: 5-11; Optimum pH: 9.5-11; Stability to pH: extremely stable at pH8-10; Reactional temperature: 10-60 deg.C; Optimum reactional temperature: 50 deg.C; Temperature stability: extremely stable below 40 deg.C; Molecular weight: 120000+ or -5000 (by sodium dodecyl sulfate electrophoresis); Affection by metallic ion: inhibited by Hg<2+> or Cd<2+>, etc.; Affection by surfactant: hardly inhibited; Affection by chelate agent: hardly inhibited by EDTA, etc.; Resistance to protease: exhibits strong resistance to alkali protease. USE:Used as enzyme for washing of tableware or clothing. PREPARATION:The objective substance is collected from the cultured substances of Bacillus sp. KSM-A P1876 (FERM P-10887) as a novel microorganism. |
