Purification and characterization of a milk clotting protease from Rhizomucor miehei

  title={Purification and characterization of a milk clotting protease from Rhizomucor miehei},
  author={S. Preetha and Rathanam Boopathy},
  journal={World Journal of Microbiology and Biotechnology},
  • S. Preetha, R. Boopathy
  • Published 1 September 1997
  • Chemistry
  • World Journal of Microbiology and Biotechnology
Benzamidine, an inhibitor of serine proteases, was used as an affinity ligand for the purification of aspartyl protease from culture filtrate of Rhizomucor miehei. The two step purification protocol (ion-exchange and affinity chromatography) resulted in a homogenous enzyme preparation with seven-fold purification and a final recovery of 22%. The purified enzyme was free of brown pigmentation, a factor inherently associated with the enzyme; it was stable and active at acidic pH (optimum pH 4.1… 

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The comparative specificity of acid proteinases.

  • I. M. VoynickJ. Fruton
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1971
The specificity of proteinases operating by a similar catalytic mechanism cannot be explained solely in terms of the amino acid residues flanking the sensitive peptide bond; in addition, the specificity includes significant contributions from secondary interactions arising from complementary relations between parts of the substrate and of the enzyme at a distance from the catalytic site.