抄録
The present study examined the enzymes responsible for proteolysis of casein in milk. Reversed-phase HPLC was used to differentiate the peptide products, of each proteinase, soluble in 12% trichloroacetic acid and in pH 4.6 milk filtrates. Peptides produced by bacterial proteinase were less hydrophobic and eluted early in the RP-HPLC chromatogram, while peptides produced by plasmin and somatic cell proteinase were more hydrophobic and eluted later. β-caseins were preferential substrates for plasmin, whereas α s-and κ-caseins were hydrolysed to a lesser extent. Proteases from bacterial origin predominantly affected κ-casein, while ß-casein and α s-casein were less susceptible. Somatic cell proteinase degraded mainly β-casein, followed by α s-casein and κ-casein. When milk was contaminated by bacterial proteinases, chromatograms of the TCA 12% filtrate showed early peaks, while the pH 4.6 filtrate showed early and late peaks when proteolysis was caused by either plasmin, somatic cell proteinase or bacterial proteinase.
