Maruo S, Kyotani Y, Yamamoto H, Miyazaki K, Ogawa H, Sakai T, Kojima M, Ezure Y
Chemistry Laboratories, Nippon Shinyaku Co., LTD., Kyoto, Japan.
Biosci Biotechnol Biochem. 1993 Aug;57(8):1294-8. doi: 10.1271/bbb.57.1294.
In repeated glycosylmoranolines synthetic reaction at 55 degrees C, cyclodextrin glycosyltransferase (CGT-ase, EC 2.4.1.19) from Bacillus stearothermophilus retained its activity for more than 600 days. A main stabilizing compound was found to be 4-O-alpha-D-glucopyranosylmoranoline. The thermostabilizing activities of moranoline, 4-O-alpha-D-glucopyranosylmoranoline, and their N-substituted derivatives were studied. Moranoline and its N-substituted derivatives stabilized glucoamylase. 4-O-alpha-D-Glucopyranosylmoranoline and its N-substituted derivatives stabilized CGT-ase and beta-amylase.
在55摄氏度的重复糖基吗啉合成反应中,嗜热脂肪芽孢杆菌的环糊精糖基转移酶(CGT酶,EC 2.4.1.19)保持其活性超过600天。发现一种主要的稳定化合物是4-O-α-D-吡喃葡萄糖基吗啉。研究了吗啉、4-O-α-D-吡喃葡萄糖基吗啉及其N-取代衍生物的热稳定活性。吗啉及其N-取代衍生物使葡糖淀粉酶稳定。4-O-α-D-吡喃葡萄糖基吗啉及其N-取代衍生物使CGT酶和β-淀粉酶稳定。