Abstract
A thermostable p- nitrophenyl-α- d-maltoside-hydrolysing α-glucosidase from Bacillus subtilis high-temperature growth transformant H-17 displayed maximal rates of hydrolysis for linear malto-oligosaccharides and α- and β-cyclodextrin with maltose and glucose as the final products. Starch, amylose, and amylopectin were degraded slowly to maltose in an exo-fashion by preferential cleavage of maltose units from the nonreducing ends. The K m values for maltoheptaose, α-cyclodextrin, starch, and amylopectin were 0.91 m m, 0.93 m m, 22 mg/ml, and 20 mg/ml, respectively. Based on substrate specificity and affinity, we have reclassified this enzyme as a cyclomaltodextrinase (E.C. 3.2.1.54).
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