[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.
D002241:Carbohydrates / Q000032:analysis; D004355:Drug Stability; D005632:Fructose / Q000302:isolation & purification / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013393:Sucrase / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature; D043324:beta-Fructofuranosidase
D002241:Carbohydrates; D005632:Fructose; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; D013393:Sucrase
Vydelenie i izuchenie svoĭstv beta-fruktozuranozidazy iz drozhzheĭ Saccharomyces cerevisiae.