Abstract
A pullulan hydrolase of Bacillus stearothermophilus KP 1064 was purified homogeneously. The molecular weight, Stokes radius, sedimentation coefficient (s20, w), extinction coefficient at 280 nm and pH 6.8, and isoelectric point were estimated as 115,000, 4.16 nm, 5.5 S, 1.92 cm2·mg-1 and 4.4, respectively. The enzyme consisted of two identical subunits each comprising a methionine residue at the NH2-terminus. The enzyme hydrolysed pullulan, amylopectin, soluble starch, amylose, α-and β-limit dextrins, α- and β-cyclodextrins, phenylα-d-maltoside, maltotriose, and maltopentaose. The main products from amylose and pullulan were maltose and panose, respectively. The substrate specificity, along with the pattern of products, suggested the assignment of the enzyme to a unique type of maltogenic α-amylase (1,4α-d-glucan glucanohydrolase, EC. 3.2.1.1).
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