PMID: 2495817May 1, 1989Paper

Specificity of milk-clotting enzymes towards bovine kappa-casein

Biochimica Et Biophysica Acta
H B Drøhse, B Foltmann

Abstract

Limited proteolysis of bovine kappa-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 kappa-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.

References

Nov 16, 1987·European Journal of Biochemistry·J CooperM Szelke
Jun 1, 1973·European Journal of Biochemistry·J C MercierB Ribadeau-Dumas
Dec 3, 1968·Biochimica Et Biophysica Acta·J JollèsP Jollès

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Citations

Dec 1, 1992·Applied Biochemistry and Biotechnology·L B ArecesO Cascone
May 4, 2016·Revista iberoamericana de micología·Virginia Mandujano-GonzálezYuridia Mercado-Flores
Sep 18, 2001·Journal of Agricultural and Food Chemistry·V GagnaireJ Léonil

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