Hydrolysis of Dairy and Meat Substrates by Chicken vs. Porcine Pepsin

Commercial hydrolysis requires maximizing product yields while minimizing operational costs. This article describes the optimal parameters for pepsin-catalyzed hydrolysis (enzyme origin, temperature, and pH) to achieve the highest efficiency using biologically valuable whey, casein, and meat protein substrates.
WPC-80 whey protein concentrate (79.05% protein), sodium caseinate (93.70% protein), and dry bovine heart powder (76.0% protein) served as substrates. The hydrolysis involved porcine and chicken pepsin preparations at temperatures ranging from 35 to 50°C and a pH range of 2.0–4.0. The degree of hydrolysis was spectrophotometrically assessed based on the content of TCAsoluble products. The statistical analysis relied on a two-way analysis of variance (ANOVA).
Within the pH range of 2.0–4.0, the highest yield of casein and meat protein hydrolysates occurred at pH 2.0. For the whey protein substrate, the peak yields were observed at pH 2.9 using chicken pepsin and at pH 2.3 using porcine pepsin. Increasing the temperature from 35 to 50°C consistently enhanced the yield of hydrolysis products. Although pH 2.0 corresponded to the highest initial enzyme activity, the hydrolysis of dairy proteins was less effective due to the compact native structure of whey proteins and the formation of casein aggregates at this pH.
Pepsins proved to be highly effective for hydrolyzing meat proteins as substrate accessibility increased significantly at pH 2.0. Consequently, these enzymes can be recommended for the commercial hydrolysis of denatured and aggregated meat proteins subjected to intense thermal treatment.

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