Akademik Veri Yönetim Sistemi
Journal of Food Measurement and Characterization, 2026 (SCI-Expanded, Scopus)
This study aimed to elucidate how enzyme type (Neutrase or Flavourzyme) influences the structural characteristics and functional properties of bioactive peptides produced from casein obtained from skimmed commercial cow’s milk (CoC). Compared with Neutrase, Flavourzyme demonstrated greater proteolytic potential, resulting in more extensive peptide formation and a distinct peptide distribution profile. After 12 h of enzymatic digestion, the Flavourzyme-treated hydrolysate (CoCF) exhibited the highest degree of hydrolysis (56.17 mg tryptone/g sample) and free amino acid content (90.52 mg AA/g sample). Hydrolysis markedly modified the peptide molecular size distribution, reducing the abundance of high molecular weight fractions (MW > 2.5 kDa) while increasing the proportion of oligopeptides (MW: 0.5–2.5 kDa), which reached 68.9% in CoCF and 70.0% in CoCN. Both enzyme treatments enhanced the bioactive potential of the casein hydrolysates, where CoCF showed superior α-amylase (78.26%), ACE (78.1%), and lipase (19.74%) inhibitory activities, as well as the highest antioxidant activity (33.21 mg TE/g sample). FTIR analysis confirmed structural rearrangements in the amide II region following hydrolysis. Collectively, these results provide evidence of the potential of enzyme-modified casein hydrolysates as multifunctional dairy ingredients for health-oriented formulations, particularly those targeting metabolic conditions such as hyperglycemia, dyslipidemia, hypertension, and obesity.