Isolation and partial characterization of globulin from Cassava (<i>Manihot esculenta</i> Crantz) tubers

Abstract

Soluble globulin was isolated using an extraction buffer (0.4 M NaCl in 35 mM potassium phosphate buffer, pH 7.6 with 0.02% Na azide). The isolated globulin was subjected to solubility tests with different NaCl concentrations. It has the highest solubility in 1.25M NaCl (1.09%), but no significant differences existed among the NaCl concentrations by analysis using one-way ANOVA at a = 0.05. Three major bands existed at LOOM NaCl dissolved globulin with molecular weight ranges of 28-33kDa, 38- 43kDa, and 65-70kDa relative to BSA. Two of these bands (38-43kDa and 65-70kDa) were observed in 0.50M and 0.75M NaCl soluble globulin. The 1.25M and 1.50M NaCl concentrations gave a single band (28-33kDa) each, while no clear bands were observed in other NaCl concentrations.

Amino acid analysis revealed glutamic acid (12.09%) as the most abundant amino acid component of cassava globulin. Nine (9) essential amino acids were present. Of these nine, lysine (10.50%) is the most predominant. Cystine (0.39%) has the lowest percentage, followed by methionine (1.76%).