[Ion exchange purification of some enzymes on KMT carboxyl cation exchanges].
Highly purfied preparations of the enzymes--yeast beta-fructofuranosidase, fungal beta-galactosidase and bacterial proteases have been isolated from crude preparations or culture liquids by adsorption on KMT microporous carboxyl cation exchanger. During desorption the enzyme activity has fully recovered and the specific activity increased 4.5-fold for beta-galactosidase and 54-fold for proteases.
D001412:Bacillus subtilis / Q000201:enzymology*; D002411:Cation Exchange Resins; D002852:Chromatography, Ion Exchange / Q000379:methods; D005696:Galactosidases / Q000302:isolation & purification*; D006026:Glycoside Hydrolases / Q000302:isolation & purification*; D003904:Mitosporic Fungi / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D012440:Saccharomyces / Q000201:enzymology*
D002411:Cation Exchange Resins; D005696:Galactosidases; D006026:Glycoside Hydrolases; D010447:Peptide Hydrolases
Ionoobmennaia ochistka nekotorykh fermentov na karboksil'nykh kationitakh tipa KMT