To confirm the identity of AmyASS, it is necessary to examine the range of substrate hydrolysis and the product profile of AmyASS. Apart from soluble starch (44.6 ± 2.8 U mg−1, relative activity 100%), the enzyme only cleaved amylose (38 ± 0.8%). No activity could be determined with amylopectin, pullulan and glycogen as the substrates.