Abstract
DPR, a fragment peptide of enterostatin (VPDPR) having hypocholesterolemic activity, was introduced into the three homologous sites, EPR, DYR, and DPI, in the soybean β-conglycinin α′ subunit by site-directed mutagenesis. The modified β-conglycinin was expressed in Escherichia coli and recovered in the soluble fraction. After purification on ion-exchange HPLC, the modified β-conglycinin was digested by trypsin to release integrated DPR. The yield of DPR from 1 mole of the modified β-conglycinin was 1.2 mole.