Specificity of milk-clotting enzymes towards bovine κ-casein
- 1 May 1989
- journal article
- Published by Elsevier BV in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 995 (3), 221-224
- https://doi.org/10.1016/0167-4838(89)90039-3
Abstract
Limited proteolysis of bovine κ-casein has been investigated with porcine pepsin A and C, and with the 2 microbial proteinases Mucor miehei proteinase and Endothia parasitica proteinase. The liberated C-terminal glycomacropeptide of κ-casein was isolated after precipitation in 3% trichloroacetic acid followed by high-performance gel-permeation chromatography on a TSK G3000 SW column. From amino acid analyses and N-terminal sequencing of the liberated peptide it is concluded that porcine pepsin A, C and Mucor miehei proteinase cleave the same bond as chymosin: Phe-105-Met-106 whereas Endothia parasitica proteinase cleaves the bond Ser-104-Phe-105.Keywords
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