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Purification and properties of beta-galactosidase from Alternaria tenius

Letunova, E.V.; Tikhomirova, A.S.; Shiian, S.D.; Markin, V.A.; Khorlin, A.Ia.

Biokhimiia 46(5): 911-919

1981

ISSN/ISBN: 0320-9725
PMID: 6794653
Document Number: 177602
.beta.-Galactosidase from A. tenuis was purified to homogeneity from the cultural fluid using acetone precipitation, ion-exchange chromatography on DEAE-cellulose, adsorption on hydroxylapatite and affinity chromatography on N-(.beta.-D-galactopyransosyl-thiocarbamoyl)-.beta.-aminocaproyl-AN-Sepharose 4B. The enzyme homogeneity was demonstrated by ultracentrifugation and polyacrylamide gel electrophoresis with SDS have no effect on the .beta.-galactosidase activity. Galactose acts as a competitive inhibitor, while glucose has no inhibiting effect on the enzyme activity.

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