Abstract
β-D-Galactosidase (EC 3.2.1.23) from ripe plantain fruit was partially purified and characterized. Purification was carried out using ammonium sulphate precipitation and gel-filtration on Sephadex G25-150 and G-25M. The enzyme displayed activity against p-nitrophenyl-β-D-galactopyranoside, with a Km of 1 mM. It was inhibited by galactose and mercuric chloride. Galactose was a noncompetitive inhibitor, while mercuric chloride was an uncompetitive inhibitor.
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