Abstract
A recombinant soyacystatin (r-soyacystatin) was tested for its inhibitory activity against cysteine proteinase of Pacific whiting and its activity was compared to that of egg white cystatin. A recombinant soyacystatin expressed in Escherichia coli was purified to electrophoretic homogeneity using phenyl-Sepharose and DEAE-Sepharose. Native egg white cystatin was purified by using affinity chromatography on CM-papain-Sepharose generated in our lab. Egg white cystatin and soyacystatin were tested for proteinase inhibitory activity against commercial papain and also cathepsin L purified from Pacific whiting muscle. The r-soyacystatin exhibited papain-like protease inhibition activity comparable to that of the egg white cystatin, which could inhibit papain and Pacific whiting cathepsin L. The r-soyacystatin subsequently inhibited the autolytic activity of Pacific whiting surimi.
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