Enzymatic Glucosylation of Salidroside from Starch by alpha-Amylase
Enzymatic Glucosylation of Salidroside from Starch by alpha-Amylase
复制标题
α-淀粉酶对淀粉中的红景天苷进行酶促糖基化
DOI:
10.1021/acs.jafc.8b06618
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发表时间:
2019
影响因子:
6.1
通讯作者:
Lu Lili
中科院分区:
文献类型:
--
作者:
Wang Ke;Qi Tingting;Guo Longcheng;Ma Zhongxuan;Gu Guofeng;Xiao Min;Lu Lili
α-Amylases are among the most important and widely used industrial enzymes for starch processing. In this work, an α-amylase fromBacillus subtilisXL8 was purified and found to possess both hydrolysis and transglycosylation activities. The optimal pH and temperature for starch hydrolysis were pH 5.0 and 70 °C, respectively. The enzyme could degrade soluble starch into beneficial malto-oligosaccharides ranging from dimer to hexamer. More importantly, it was able to catalyze α-glycosyl transfer from the soluble starch to salidroside, a medicinal plant-derived component with broad pharmacological properties. The transglycosylation reaction catalyzed by the enzyme generated six derivatives in a total high yield of 73.4% when incubating with 100 mg/mL soluble starch and 50 mM salidroside (pH 7.5) at 50 °C for 2 h. These derivatives were identified as α-1,4-glucosyl, maltosyl, maltotriosyl, maltotetraosyl, maltopentaosyl, and maltohexaosyl salidrosides, respectively. They were novel promising compounds that might integrate the bioactive functions of malto-oligosaccharides and salidroside.