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- W2032598678 abstract "Abstract 1. 1.|α-Glucosidase (α- d -glucoside glucohydrolase, EC 3.2.1.20) from Mucor rouxii was purified by treatment which included heat shock, precipitation with protamine sulfate, (NH 4 ) 2 SO 4 and ethanol, and chromatography on DEAE-Sephadex and Sephadex G-200. 2. 2.|Purity of the enzyme was assessed by gel chromatography and polyacrylamide gel electrophoresis. Only one band of protein was observed. 3. 3.|The enzyme appeared to be a glycoprotein containing 40% carbohydrate. Glucose and, to a lesser extent, galactose and fucose were identified in acid hydrolysates of the enzyme. The enzyme behaved as a cation at acid pH but not as an anion at alkaline pH. It is suggested that possibly carboxylic groups from aspartate and/or glutamate are blocked. 4. 4.|The optimum pH with phosphate buffer was found to be 3.5 and the optimum temperature 50–60°. The enzyme was highly specific. It failed to hydrolyse several disaccharides and synthetic α-glucosides. It hydrolysed maltose and starch only. The sole product formed from maltose was glucose. Glucose inhibited enzymatic activity, whereas glucosamine had no effect." @default.
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- W2032598678 date "1972-02-01" @default.
- W2032598678 modified "2023-09-26" @default.
- W2032598678 title "Purification and characterization of α-glucosidase from Mucor rouxii" @default.
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- W2032598678 doi "https://doi.org/10.1016/0005-2744(72)90241-0" @default.
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