Enzymatic Hydrolysis of Camel Milk Proteose-Peptones: Generation of Bioactive Peptides with Antioxidant, Antibacterial, and Techno-Functional Properties

Abstract Bioactive peptides derived from camel milk proteins, particularly caseins and whey proteins, have been extensively investigated, whereas the proteose-peptone (PPT) fraction remains largely unexplored. This study aimed to generate and characterise bioactive peptides released from camel milk PPT following enzymatic hydrolysis. PPT was hydrolyzed using pepsin, trypsin, and chymotrypsin (E/S = 1%, 37 °C, 4 h), and the resulting hydrolysates were evaluated for their degree of hydrolysis (DH), antioxidant activity (DPPH and ABTS assays), antibacterial activity, and techno-functional properties. Pepsin exhibited the highest proteolytic efficiency, reaching a DH of 3.32%, followed by chymotrypsin (2.76%) and trypsin (2.09%). Antioxidant activity was significantly enhancedafter hydrolysis, with the peptic hydrolysate showing the lowest IC₅₀ values (DPPH: 57.80 mg/mL; ABTS: 54.87 mg/mL) compared with tryptic (69.36 and 60.41 mg/mL) and chymotryptic hydrolysates (70.34 and 59.40 mg/mL). The peptic hydrolysate also demonstrated antibacterial activity against Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 25923 (MIC = 20 mg/mL; MBC = 80 mg/mL). In contrast, tryptic hydrolysates exhibited superior techno-functional performance, with an emulsifying activity index of 28.44 m2/g and a foaming capacity of 166.66%. Overall, camel milk PPT represents a promising source of multifunctional bioactive peptides with potential applications as natural functional ingredients in food systems.