Purification of recombinant cathepsin C (CTC) from the fermentation broth of methylotrophic yeast, Candida boidinii was conducted. After centrifugation, fermentation supernatant was processed with four consecutive chromatography columns (cation exchange, hydrophobic, anion exchange, and gel filtration). As a result, the recombinant CTC of 4.7 U/mg was purified from the fermentation broth containing 169 U/l of CTC and the yield was 35%. From the gel filtration analysis, molecular weight of the recombinant CTC was determined to be about 200 kDa, that was almost the same as the native one. From SDS-PAGE analysis and N- terminal amino acid analysis, the monomer bands of the recombinant CTC were discussed. In order to compare the enzymatic property of the recombinant and native CTC, (1) pH profile of the activities, (2) temperature profile of the activities, and (3) enzymatic specificity for several substrates were investigated. From these studies, it was revealed that the enzymatic property of the recombinant CTC was almost the same as that of the native one.