Some Effects of Hydrogen Peroxide on Casein and Its Implications in Cheese Making

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Abstract
The activity of the proteolytic enzymes, trypsin, pepsin, and rennin, against hydrogen peroxide-catalase-treated caseins, and the behavior of H2O2,-treated casein in the presence of various ions, particularly Ca were investigated. Prior treatment of casein with H2O2-catalase as applied to milk for cheese making, used in larger than normal levels, increases proteolysis, especially that by rennin. The greatest hydrolysis occurred in treated protein, soluble at pH 4.6, after rennin action. Treated samples were hydrolyzed 3 times faster than controls and attained a final solubility 3 times greater. Hydrogen peroxide treatment of casein results in significant behavior changes in the presence of calcium ions. When Ca++ is present, the solubility of H2O2-treated protein over that of the control at pH 6.5 is slightly increased but, at pH 4.6, a considerably greater solubility increase is observed. The increased solubility is due mainly to alterations in [beta]-casein, which undergoes similar changes when an isolated preparation is treated with H2O2. The increased softness of Cheddar cheese body noted in cheese from hydrogen peroxide-catalase-treated milks may be due, in part, to this higher susceptibility of its protein to proteolysis and, in part, at early ripening stages, to the increased solubility of H2O2 -treated calcium caseinate.

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