SUMMARY: Four species of the genus , especially and , produced amylase when grown in liquid medium containing starch. The amylase was purified nearly 1200-fold with a 36% yield from the culture supernatant of by ammonium sulphate precipitation, CM-52 cellulose chromatography and gel filtration. An of 47000–49000 was estimated for the enzyme from results of SDS-PAGE and glycerol gradient centrifugation, respectively. Metal ions such as Mg, Ca, Mn or Zn are not required for activity. The amylase is active from pH 5.0 to 7.5, degrades starch endohydrolytically and has a of 2.08 mg starch ml. Amylopectin, amylose and glycogen were also hydrolysed. Dextran, maltose, maltotriose, maltotetraose and 4-nitrophenyl α--glucoside were hydrolysed very slowly, or not at all. Other enzymes capable of degrading starch, maltose or malto-oligosaccharides were not detected in the culture supernatant of


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