Purification and characterization of heterogeneous glucoamylases from Monascus purpureus.
Two forms of an extracellular glucoamylase, MpuGA-I and MpuGA-II, were purified to homogeneity from Monascus purpureus RY3410. The molecular weights of these enzymes were estimated to be 60,000 (MpuGA-I) and 89,000 (MpuGA-II). These enzymes were glycoproteins with a carbohydrate content of 15.0% (MpuGA-I) and 16.2% (MpuGA-II) respectively. The pH optima were 5.0 for both enzymes, and the optimal temperatures were 50 degrees C (MpuGA-I) and 65 degrees C (MpuGA-II). The Km values for soluble starch were calculated to be 4.0+/-0.8 mg/ml (MpuGA-I) and 1.1+/-0.2 mg/ml (MpuGA-II) respectively.
Tachibana
Shinjiro
S
Department of Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus, Japan.
Yasuda
Masaaki
M
D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D005087:Glucan 1,4-alpha-Glucosidase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007526:Isoelectric Point; D007700:Kinetics; D019216:Metals, Heavy / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D032741:Monascus / Q000201:enzymology*; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D012995:Solubility; D013213:Starch / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D002241:Carbohydrates; D019216:Metals, Heavy; D013213:Starch; D005087:Glucan 1,4-alpha-Glucosidase