Comparative study of soybean plasteins synthesized with soluble and immobilized .alpha.-chymotrypsin

Plasteins were prepared from low molecular weight peptides of a peptic digest of soybean protein. The plasteins were fingerprinted on silica gel by a combination of electrophoresis and TLC, eluted, hydrolyzed, and subjected to amino acid analysis. The results indicated that the plasteins from soluble alpha -chymotrypsin were richer in glycine, valine, leucine, and serine than the plastein prepared from immobilized alpha -chymotrypsin. Plasteins prepared from immobilized alpha -chymotrypsin were rich in glutamic acid, lysine, alanine, and threonine, suggesting a much more hydrophilic plastein than prepared from the soluble form of the enzyme.