Properties of the raw-starch digesting amylase of Aspergillus sp. K-27: a synergistic action of glucoamylase and alpha-amylase.
Glucoamylase and alpha-amylase have been purified from a crude enzyme preparation of Aspergillus sp. K-27. The former was thermostable and seemed to have a "starch-binding site", judging from the results of a kinetic study, and the latter synergistically enhanced the degradation of starch granules with glucoamylase.
D001230:Aspergillus / Q000201:enzymology*; D005087:Glucan 1,4-alpha-Glucosidase / Q000302:isolation & purification / Q000378:metabolism*; D005959:Glucosidases / Q000378:metabolism*; D007700:Kinetics; D013213:Starch; D013379:Substrate Specificity; D000516:alpha-Amylases / Q000302:isolation & purification / Q000378:metabolism*
D013213:Starch; D005959:Glucosidases; D000516:alpha-Amylases; D005087:Glucan 1,4-alpha-Glucosidase