In order to suppress autolysis which decreases recovered activity), synthesized inhibitor is applied to protease refolding. In the refolding of Streptomyces griseus trypsin (SGT) from its denatured and reduced state, recovered activity) reaches only 15% by the ordinary dilution method, while it exceeds 60% in the presence of the gel on which p-aminobenzamidine, an inhibitor to trypsin, is immobilized covalently. Furthermore, by use of the immobilized inhibitor, purification and recovery of renatured SGT are efficiently performed. In addition, aggregation, the other disadvantageous reaction to renaturation, can also be diminished with coexistence of 1 M urea in this suspension system. Reusability of the immobilized inhibitor will make it possible to develop this refolding into the continuous process.