Purification and characterization of an alkaline protease Prot 1 from Botrytis cinerea : biodetergent catalyst assay.

@article{Abidi2007PurificationAC,
  title={Purification and characterization of an alkaline protease Prot 1 from Botrytis cinerea : biodetergent catalyst assay.},
  author={Ferid Abidi and Ferid Limam and Mohamed N{\'e}jib Marzouki},
  journal={Applied biochemistry and biotechnology},
  year={2007},
  volume={141 2-3},
  pages={361-76}
}
Alkaline thiol protease named Prot 1 was isolated from a culture filtrate of Botrytis cinerea. The enzyme was purified by ammonium sulfate fractionation, gel filtration, and ion-exchange chromatography. Thus, the enzyme was purified to homogeneity with specific activity of 30-fold higher than that of the crude broth. The purified alkaline protease has an apparent molecular mass of 43 kDa under denaturing conditions as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The… CONTINUE READING