The action pattern of Bacillus subtilis alpha-amylase on Jewel variety sweet potato starch, amylose and amylopectin was monitored using high performance size exclusion chromatography. A wide range of products, from high molecular weight polysaccharides to specific saccharides of low molecular weights, were observed. The hydrolysis pattern for amylose in starch was concealed by hydrolytic fragments formed from amylolysis of the greater quantity of amylopectin. Amylopectin was degraded to a more specific mixture of polysaccharide fragments. Changes in molecular size of hydrolytic fragments formed during amylolysis supported the cluster model previously proposed for amylopectin. These results also suggest that the action of alpha-amylase on sweet potato starch is generally a nonrandom process, primarily resulting from enzymatic action on amylopectin. To support this hypothesis, a more random pattern of hydrolysis was observed from acid treated starch.
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Rupp et al. (1988) studied this question.
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