Enzymatic Glucosylation of Salidroside from Starch by α-Amylase

α-Amylases are among the most important and widely used industrial enzymes for starch processing. In this work, an α-amylase from Bacillus subtilis XL8 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.