SEPARATION OF AN α-GALACTOSIDASE FROM WATERMELON SEEDS

Abstract

An α-galactosidase from watermelon seeds has been separated from invertase and β-galactosidase by ammonium sulphate precipitation followed by elution from a DEAE-cellulose column with phosphate buffers. This enzyme is capable of hydrolyzing galactose residues from melibiose, raffinose, and stachyose. The pH optimum with the three substrates is close to 4.2. The enzyme is inhibited by the products of the reaction, and, in the case of melibiose, by the substrate itself.