[Purification and characterization of beta-fructofuranosidase from yeast Saccharomyces cerevisiae].
Copyright policy )[Purification and characterization of beta-fructofuranosidase from yeast Saccharomyces cerevisiae].
Intracellular invertase was isolated from the yeast Saccharomyces cerevisiae, race XI, and purified by ion-exchange chromatography on DEAE-cellulose and gel-filtration on Sephadex G-200. The effect of pH, temperature, metal ions, thiolic agents, and EDTA on the enzyme activity and stability was investigated. The enzyme was estimated to have a molecular weight of 270 000 and a carbohydrate content of 20--30%. By disc-electrophoresis and isoelectric focusing the highly purified enzyme was found to be heterogenous. Its molecular forms had isoelectric points at 3.0, 4.0, 4.5, and 4.9.
Molecular Weight, Kinetics, Drug Stability, Glycoside Hydrolases, beta-Fructofuranosidase, Carbohydrates, Temperature, Fructose, Saccharomyces cerevisiae, Isoelectric Focusing, Sucrase
Molecular Weight, Kinetics, Drug Stability, Glycoside Hydrolases, beta-Fructofuranosidase, Carbohydrates, Temperature, Fructose, Saccharomyces cerevisiae, Isoelectric Focusing, Sucrase
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