Abstract
Purification and Determination of Inhibitory Activity of Recombinant Soyacystatin Against Papain and Fish Protease
Recombinant (r-) soyacystatin was characterized for its inhibitory activity against papain and compared to egg white cystatin. r-Soyacystatin expressed in E. coli was purified with phenyl-Sepharose and DEAE 4.33 fold as a recombinant protein. Egg white cystatin was purified by using affinity chromatography on cm-papain-Sepharose. Inhibitory activity of r-soyacystatin was similar to that of egg white cystatin. The amount required to inhibit 50% activity of papain used in the assay, 2 pg, was 0.245 |ig and 0.310 jag for soyacystatin and egg white cystatin, respectively. r-Soyacystatin inhibited 90% of autolytic activity in fish muscle.
Keywords
soyacystatin egg white cystatin proteolytic activity protein purification
