Akademik Veri Yönetim Sistemi
Journal of Food Measurement and Characterization, 2026 (SCI-Expanded, Scopus)
Cow (CWPC), water buffalo (WBWPC), goat (GWPC), and sheep (SWPC) whey protein concentrate hydrolysates were generated using Flavourzyme (CWPCF, WBWPCF, GWPCF, and SWPCF) and Neutrase (CWPCN, WBWPCN, GWPCN, and SWPCN), each for 12 h, and investigated with respect to the selected bioactivities, free amino acids, molecular weight distribution, etc. Comparative results revealed significant variations among species and enzymes. Neutrase demonstrated more potent effects in characterizing bioactive peptides. In contrast, Flavourzyme was more effective in increasing the free amino acid content, with CWPCF exhibiting the highest value (27.64 mg AA/g whey). SWPCF and GWPCN exhibited the highest and lowest degrees of hydrolysis at 49.09 and 10.95 mg tryptone/g whey, respectively. The molecular weights of the peptides in the samples decreased sharply after the enzymes were used. Oligopeptides (0.5 and 2.5 kDa) accounted for a significant fraction of the hydrolysates, ranging from 84 to 39% across all samples. On the other hand, Fourier-transform infrared spectra revealed enhancements in the hydrolysates in the amide I and II bands. The samples treated with Neutrase showed higher antioxidant activity than those treated with Flavourzyme or untreated. GWPCN (47.98%) and WBWPCF (45.80%) showed the greatest pancreatic lipase inhibition. WBWPC exhibited the strongest α-amylase inhibition (87.2%), closely followed by WBWPCN (87.1%), while the SWPCN (99.8%) and CWPCN (92.6%) demonstrated the highest ACE inhibition activity values. Overall, this study highlighted that whey protein concentrate hydrolysates could be valuable sources of low-molecular-weight peptides peptides, which can be utilized in the management of chronic diseases and in the production of value-added food products for athletes and infants.