Purification and properties of alpha-galactosidase isosymes from Phlebia radiata
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Updated: Sep 20, 2026
Elucidating β-1,3-Glucanase and Peroxidase Physicochemical Properties of Wheat Cell Wall Defense Mechanism Against Diuraphis noxia Infestation
Published on: July 26, 2024
Monika Prendecka1, Krystyna Szyjka, Jerzy Rogalski
1Department of Biochemistry, Maria Curie-Skłodowska University, M. C.-Skłodowska Place 3, 20-031 Lublin, Poland.
Abstract:
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.
