Purification and Characterization of 56 kDa cold active Protease from Serratia marcescens (original) (raw)
2011, African Journal of Microbiology Research
The extracellular cold active protease produced from Serratia marcescens TS1. The protease was purified to homogeneity from the production medium by ammonium sulphateation then followed by acetone precipitation with 80% saturation. The cold active protease was fractionized by diethylaminoethyl (DEAE) cellulose column chromotography. The molecular weight of protease was approximately 56 KDa. The isoelectric point was close to 6.4. The maximal activity towards casein was found at 40°C and its pH activity was at 8.0. The protease was strongly inactivated by HgCl 2 metal ion and reactivated by FeSO 4 thus indicated as metalloprotease. The protease was inhibited by Na 2 ethylenediaminetetraacetic acid (EDTA). The protease of S. marcescens TS1 showed a potential application in the laundry industry by removeing the blood, chocolate and egg youlk stains from the white cotton cloths in a short period without changing texture of cloths.
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