Abstract
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.
MeSH terms
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Amino Acid Sequence
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Carbohydrates / analysis
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Chromatography, Gel
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Electrophoresis, Polyacrylamide Gel
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Enzyme Activation / drug effects
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Enzyme Stability
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Glucan 1,4-alpha-Glucosidase / analysis
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Glucan 1,4-alpha-Glucosidase / antagonists & inhibitors
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Glucan 1,4-alpha-Glucosidase / chemistry
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Glucan 1,4-alpha-Glucosidase / isolation & purification*
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Glucan 1,4-alpha-Glucosidase / metabolism*
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Hydrogen-Ion Concentration
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Hydrolysis
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Isoelectric Point
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Kinetics
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Metals, Heavy / pharmacology
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Molecular Sequence Data
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Molecular Weight
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Monascus / enzymology*
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Phylogeny
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Sequence Homology, Amino Acid
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Solubility
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Starch / metabolism
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Substrate Specificity
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Temperature
Substances
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Carbohydrates
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Metals, Heavy
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Starch
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Glucan 1,4-alpha-Glucosidase