Kato M, Miura Y, Kettoku M, Komeda T, Iwamatsu A, Kobayashi K
a Applied Bioresearch Center , Kirin Brewery Co., Ltd ., 3 Miyaharaeho, Takasakishi, Gunma 370-12 , Japan.
b Central Laboratories for Key Technology , Kirin Brewery Co., Ltd ., 1-13-5 Fukuura, Kanazawaku, Yokohamashi, Kanagawa 236 , Japan.
Biosci Biotechnol Biochem. 1996 Jan;60(5):925-8. doi: 10.1271/bbb.60.925.
Amylolytic activity, which converts soluble starch to α,α-trehalose (trehalose), was found in the cell homogenate of the hyperthermophilic acidophilic archaeum, Sulfolobus solfataricus KM1. Two enzymes, a glycosyltransferase and an α-amylase, which were essential for this activity were identified. The α-amylase was purified to homogeneity on SDS-PAGE. The α-amylase catalyzed the hydrolysis of glycosyltrehaloses to trehalose. Analysis of the reaction products, kinetic parameters, and experimental findings using (3)H-labeIed substrates indicated that the α-amylase hydrolyzed only the α-1,4 glucosidic linkage adjacent to the trehalose unit of the glycosyltrehaloses. Six strains of the Sulfolobaceae family examined were observed to have the glycosyltrehalose-hydrolyzing enzyme, the α-amylase.
在嗜热嗜酸古菌嗜热栖热菌KM1的细胞匀浆中发现了将可溶性淀粉转化为α,α-海藻糖（海藻糖）的淀粉酶活性。鉴定出了两种对该活性至关重要的酶，一种糖基转移酶和一种α-淀粉酶。α-淀粉酶在SDS-PAGE上纯化至同质。α-淀粉酶催化糖基海藻糖水解为海藻糖。使用(3)H标记底物对反应产物、动力学参数和实验结果进行分析表明，α-淀粉酶仅水解糖基海藻糖中海藻糖单元相邻的α-1,4糖苷键。在所检测的6株硫化叶菌科菌株中均观察到了具有糖基海藻糖水解酶活性，即α-淀粉酶。
