Enzyme Activity Measurement of Pullulanase

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Pullulanases (pullulan 6-glucanohydrolase, EC 3.2.1.41) are debranching enzymes that are able to hydrolyze the α-1,6-glycosidic linkage in pullulan, starch, amylopectin, and related oligosaccharides. Pullulanases can be divided into two groups, mainly according to their substrate preference. Type I pullulanases specifically cleave the α-1,6-glycosidic linkages in pullulan and branched oligosaccharides to produce maltotriose and linear oligosaccharides, respectively. Type II pullulanases, also known as amylopullulanases, can hydrolyze both α-1,6-glycosidic linkages and α-1,4-glycosidic linkages in branched and linear oligosaccharides. All of the type I pullulanases are found to belong to glycoside hydrolase family 13 (GH13), while amylopullulanases are classified in GH13 and GH57 based on the architecture of catalytic domain and number of conserved sequences.

Pullulanase can be used in many industrial processes. For example, one fast growing application is the enzymatic conversion of starch into glucose, maltose, and fructose, which serve as food sweeteners. The majority of starches used in industry consist of about 80% amylopectin, which contains 4-5% of α-1,6 glucosidic linkages. Pullulanases have been employed in starch saccharification by hydrolyzing the α-1,6 linkages in amylopectin, producing high-glucose or high-maltose syrups. Therefore, this enzyme is an indispensable part in food processing industry. There are many available methods to measure the enzyme activity, all depend on the detection of the released reducing sugar. Creative Enzymes uses the most reliable spectrophotometric method to achieve rapid and precise assays.

Figure: The crystal structure of pullulanase from Anoxybacillus sp.
Reference: Jianyong Xu et al. Proteins 2014 82:1685–1693.

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