Purification and characterization of a fibrinolytic enzyme produced by Bacillus sp. S19 from shrimp jeat-gal = 새우젓 유래 Bacillus sp. S19가 생산하는 혈전용해효소의 정제 및 특성

Abstract

A fibrinolytic enzyme was purified to homogeneity from Bacillus sp. S19 using DEAE and CM column chromatographies, and gel filtration with a recovery yield of 13%. Its molucular mass was stimated to be 42 kDa by SDS-PAGE. The pH and temperature optima were 8.0 abd 40°C, respectively. The enzyme was stable up to 45°C and over a pH range of 6-9. The N-terminal amino acid sequence of the enzyme was determined as Ala-Gln-Asp-Ala-Thr-Val-Asn-Ile-Ser-Ala-Glu-Arg-Gln-Val-Ile. The fibrinolytic activity was increased by Cu2+ while it was strongly inhibited by metal ions such as Cd2+ and Ba2+. In addition, the enzyme was inhibited by EDTA, but not by PMSF, suggesting that it is a metalloprotease.