Enzymes of Trichomonas foetus. Separation and properties of two β-galactosidases

Abstract

The β-galactosidase activity in extracts of Trichomonas foetus is separable into two fractions by gel filtration on Sephadex G-200. When o-nitrophenyl β-d-galactoside is used as substrate the first fraction to be eluted, β-galactosidase 1, has 50 times the activity (units per mg of protein) of the crude preparation. This fraction is activated by Mn2+ and Co2+ and inhibited by Hg2+ and EDTA. In the presence of Mn2+ the pH optimum for the hydrolysis of o-nitrophenyl β-d-galactoside or lactose is 5.8–6.0. β-Galactosidase 1 is an exoglycosidase that releases β-linked galactose joined to aliphatic and various carbohydrate aglycones. Hydrolysis is prevented, however, by a substituent on either the subterminal sugar or the terminal non-reducing β-galactosyl residue in an oligosaccharide. The second fraction, β-galactosidase 2, is not activated by metal ions or inhibited by EDTA and has a broad pH optimum from 4.5 to 6.0.