Purification and Characterization of Heterogeneous Glucoamylases fromMonascus purpureus
Copyright policy )Purification and Characterization of Heterogeneous Glucoamylases fromMonascus 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.
Molecular Sequence Data, <I>Monascus purpureus</I>, Carbohydrates, glucoamylase, Substrate Specificity, Metals, Heavy, Enzyme Stability, fermented tofu, Amino Acid Sequence, Isoelectric Point, Phylogeny, Sequence Homology, Amino Acid, Hydrolysis, Starch, Hydrogen-Ion Concentration, Monascus, Enzyme Activation, Molecular Weight, Kinetics, Solubility, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Glucan 1,4-alpha-Glucosidase, tofuyo, red koji
Molecular Sequence Data, <I>Monascus purpureus</I>, Carbohydrates, glucoamylase, Substrate Specificity, Metals, Heavy, Enzyme Stability, fermented tofu, Amino Acid Sequence, Isoelectric Point, Phylogeny, Sequence Homology, Amino Acid, Hydrolysis, Starch, Hydrogen-Ion Concentration, Monascus, Enzyme Activation, Molecular Weight, Kinetics, Solubility, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Glucan 1,4-alpha-Glucosidase, tofuyo, red koji
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