Abstract
The substrate specificity of a neutral α-glucosidase was investigated. The enzyme was active especially on malto-oligosaccharides, phenyl-α-maltoside and nigerose. The action on isomaltose and phenyl-α-glucoside was too weak. Isomalto-oligosaccharides made up of three or more glucose units were not attacked. The α-glucans, such as amylopectin, β-limit dextrin, glycogen and amylose besides soluble starch, also were hydrolyzed.The ratio of velocity of hydrolysis for maltose, nigerose, phenyl-α-maltoside, maltotriose and maltotetraose was estimated to be 100: 89: 93: 74: 80 in this order. The extraporated Km values for maltose, nigerose, phenyl-α-maltoside, maltotriose and maltotetraose were 2.1 mm, 20.0 mm, 0.33 mm, 0.28 mm and 0.15 mm, respectively. The enzyme is considered to be essentially a neutral α-glucosidase with a preferential activity on malto-oligosaccharides.
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