Kato M, Miura Y, Kettoku M, Shindo K, Iwamatsu A, Kobayashi K
Applied Bioresearch Center, Kirin Brewery Co., Ltd., Gunma, Japan.
Biosci Biotechnol Biochem. 1996 Mar;60(3):546-50. doi: 10.1271/bbb.60.546.
Amylolytic activity that converts soluble starch to alpha, alpha-trehalose (trehalose), was found in the cell homogenate of the hyperthermophilic acidophilic archae, Sulfolobus solfataricus KM1. DEAE chromatography of the homogenate as well as other new reliable assay methods showed two enzymes to be essential for this activity. These enzymes, a glycosyltransferase and an amylase, were purified to homogeneity and characterized. Their molecular masses were 76 kDa and 61 kDa and activities were maximal at 70-80 degrees C and 70-85 degrees C, respectively. High thermostability was noted for each. The reaction products by the two enzymes on maltooligosaccharides were identified by 1H- and 13C-NMR spectra and HPLC analysis. The cooperative mechanism of the two enzymes was used in a new enzymatic pathway for trehalose synthesis from starch.
在嗜热嗜酸古菌硫化叶菌KM1的细胞匀浆中发现了能将可溶性淀粉转化为α,α-海藻糖（海藻糖）的淀粉酶活性。对匀浆进行二乙氨基乙基纤维素（DEAE）色谱分析以及其他新的可靠检测方法表明，有两种酶对该活性至关重要。这两种酶，一种是糖基转移酶，另一种是淀粉酶，已被纯化至同质并进行了特性鉴定。它们的分子量分别为76 kDa和61 kDa，活性分别在70 - 80℃和70 - 85℃时达到最大值。每种酶都具有很高的热稳定性。通过1H-和13C-核磁共振光谱以及高效液相色谱分析确定了这两种酶作用于麦芽寡糖的反应产物。这两种酶的协同机制被用于一种从淀粉合成海藻糖的新酶促途径。
