Purification and properties of alpha-galactosidase isosymes from Phlebia radiata.
Phlebia radiata formed extracellular alpha-galactosidase when it was grown in a culture containing wheat bran or locus bean gum as a carbon source. Their activities were optimal at pH 5.0, and demonstrated the highest level of activity at 60 degrees C. Highly purified isoforms of alpha-galactosidase (AGaS-m1, AGaS-m2, AGaS-m3) isolated from the media with galactomannan and (AGaS-b1, AGaS-b2, AGaS-b3) from the media with wheat bran were obtained by means of the column chromatography on Q-Sepharose and chromatofosussing on Polybuffer Exchanger PBE-94.
Prendecka
Monika
M
Department of Biochemistry, Maria Curie-Skłodowska University, M. C.-Skłodowska Place 3, 20-031 Lublin, Poland.
Szyjka
Krystyna
K
Rogalski
Jerzy
J
D002852:Chromatography, Ion Exchange; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D020072:Polyporales / Q000201:enzymology*; D000519:alpha-Galactosidase / Q000302:isolation & purification* / Q000378:metabolism
D007527:Isoenzymes; D000519:alpha-Galactosidase