Abstract:
Alpha- galactosidase extracted from coconut endosperm was purified to homogenity as determined by polyacrylamide gel electrophoresis by affinity chromatography using adsorbants. Large scale purification was done by hydrophobic chromatography. Purified alpha galactosidase was reduced alkylated, and fragment. The peptides obtained were used for amino acid analysis. Inhibition of alpha galactosidase was seen by N-Bromosuccinamide, oxidation of two tryptophan residues, Modification of thyrosine residue and carbodiamide. But in the presence of the competitive inhibitor D- galactose the enzyme was prolected from inhibition.
