Plastein synthesis with α‐chymotrypsin immobilised on chitin

Low‐molecular weight peptide fractions were prepared from soya bean, lucerne (alfalfa) leaf protein, and wild grass leaf protein by enzymatic hydrolysis. The concentrated hydrolysates were used as substrates for plastein synthesis with α‐chymotrypsin immobilised on chitin. When submitted to gel filtration on Sephadex G‐50, the plasteins formed with the immobilised α‐chymotrypsin were comparable to the plasteins formed from the soluble enzyme. Isoelectric focusing of the plasteins showed five bands each from immobilised α‐chymotrypsin and from soluble chymotrypsin. However, slight differences in the isoelectric points of the comparable bands were observed.