PURIFICATION AND CHARACTERIZATION OF ELASTASE FROM THE PYLORIC CECA OF RAINBOW-TROUT (ONCORHYNCHUS-MYKISS)

1. An elastase-like enzyme was purified from the pyloric caeca of rain bow trout by hydrophobic interaction, cation exchange and gel-filtrati on chromatography. 2. The approximate molecular weight of the elastase was 27 kDa and the isoelectric point was remarkably basic. 3. The pH optimum of this enzyme was 8.0, when assayed with Succinyl-Ala-Ala-Ala -p-Nitroanilide. 4. When assayed with Succinyl-Ala-Ala-Ala-p-Nitroanil ide, the enzyme activity had a temperature optimum of 45-degrees-C, an d the enzyme was stable up to this temperature. 5. The trout elastase exhibited a higher specific activity than porcine elastase against Suc cinyl-Ala-Ala-Ala-p-Nitroanilide and elastin-orcein. 6. The trout elas tase was inhibited by elastatinal, PMSF, TPCK, SBTI and Bowman-Birk in hibitor.