Buonocore V, Caporale C, De Rosa M, Gambacorta A
J Bacteriol. 1976 Nov;128(2):515-21. doi: 10.1128/jb.128.2.515-521.1976.
Bacillus acidocaldarius Agnano 101 produces an inducible thermoacidophilic alpha-amylase. The enzyme production occurs during the stationary phase of growth in the presence of compounds with alpha-1,4-glucosidic linkages. The enzymatic activity is both present in the culture medium and associated with the cells; the enzymes purified from both sources show identical molecular and catalytic properties. The purified amylase has a single polypeptide chain of molecular weight 68,000 and behaves like an alpha-amylase with affinity constants for starch and related substances of 0.8 to 0.9 mg/ml. The pH and temperature optima for activity are 3.5 and 75degreesC, respectively. The amylase is stable at acidic pH (below 4.5). Its thermal stability is strictly dependent upon protein concentration; the half-life at 60degreesC of the amylase in a 70-mug/ml solution is about 5 days.
嗜酸热硫化叶菌阿尼亚诺101株产生一种可诱导的嗜热嗜酸α-淀粉酶。在生长稳定期，在具有α-1,4-糖苷键的化合物存在下会产生该酶。酶活性既存在于培养基中，也与细胞相关；从这两种来源纯化的酶显示出相同的分子和催化特性。纯化的淀粉酶具有一条分子量为68,000的单多肽链，表现得像一种α-淀粉酶，对淀粉及相关物质的亲和常数为0.8至0.9mg/ml。活性的最适pH和温度分别为3.5和75℃。该淀粉酶在酸性pH（低于4.5）下稳定。其热稳定性严格取决于蛋白质浓度；在70μg/ml溶液中，淀粉酶在60℃的半衰期约为5天。
