1982 Volume 46 Issue 1 Pages 7-13
Bacillus sp. 11-1S, a thermophilic acidophilic bacterial strain, produced an extracellular amylase with unusual characteristics. The enzyme was purified 40-fold by SE-Sephadex column chromatography. The pH optimum for activity was 2.0, and substantial activity was noted in the pH range of 1.5-3.5. The optimal temperature was 70°C, but the activity decreased markedly in lower reaction temperatures. Arrhenius plots of the reaction showed two straight lines intersecting at about 50°C. The activity or stability of the enzyme was not likely to depend on Ca2+. The molecular weight of the enzyme was 54, 000 calculated from the electrophoretic mobility. The enzyme behaved like an a-amylase (1, 4-α-D-glucan glucanohydrolase, E.C. 3.2.1.1). About 34% of glucosidic linkages of soluble starch was hydrolyzed at 65°C and pH 2.0, in 24 hr, and the major products were maltotriose and maltose.
This article cannot obtain the latest cited-by information.