Analysis of the Amylolytic Enzyme System of Clostridium thermosulfurogenes EM1: Purification and Synergistic Action of Pullulanases and Maltohexaose Forming α‐Amylase

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Abstract
During growth of C. thermosulfurogenes EM1 on starch, seven forms of pullulanase and one form of α‐amylase were detected after gel electrophoretic separation of proteins. By determining the isoelectric points and N‐terminal sequences of various pullulanase species it was evident that no structural differences exist between these proteins. These pullulanases hydrolyzed α‐1,4‐ and α‐1,6‐linkages in various soluble sugar polymers causing their breakdown to maltose and maltotriose. Unlike these enzymes, the α‐amylase produced by C. thermosulfurogenes EM1 preferentially attacked non‐soluble starch. The main product of hydrolysis was maltohexaose. The combined action of pullulanases and α‐amylase on native starch showed synergistic effect. This synergistic effect was not observed if soluble starch was used as substrate.
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