Effects of coagulants on peptide profiles and ACE-inhibitory activity in ultrafiltered white (Beyaz) cheese
JOURNAL OF FOOD COMPOSITION AND ANALYSIS, cilt.123, ss.1-11, 2023 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 123
- Basım Tarihi: 2023
- Doi Numarası: 10.1016/j.jfca.2023.105622
- Dergi Adı: JOURNAL OF FOOD COMPOSITION AND ANALYSIS
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, PASCAL, Analytical Abstracts, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Food Science & Technology Abstracts, Veterinary Science Database
- Sayfa Sayıları: ss.1-11
- Açık Arşiv Koleksiyonu: AVESİS Açık Erişim Koleksiyonu
- Süleyman Demirel Üniversitesi Adresli: Evet
Özet
The present study aimed to evaluate the effects of two different enzymes, one derived from microbial sources and the other from animal sources, on the peptide profile with low molecular weight (<3 kDa) and ACE-inhibitory activity of White (Beyaz) cheese produced from ultrafiltered (UF) milk. The control group's cheeses were produced using pasteurized milk. Throughout the 90-day ripening period, the coagulating enzyme demonstrated no significant effects on the dry matter and protein values (p > 0.05). The protein content of < 3 kDa peptide extracts changed ripening, with no statistically significant effects attributed to the enzyme variation (p > 0.05). ACE inhibition increased in all cheeses by the end of the ripening process (p < 0.05). The ACE-inhibitory activity of < 3 kDa peptide extracts obtained from the UF White cheese produced using the microbial enzyme exhibited an increase corresponding to the observed increase in the total area of RP-HPLC peaks. The LC-MS/MS analysis revealed that the animal-sourced control group yielded the highest number of β-casein and αS1-casein peptides. Many < 3 kDa peptides described in the present possessed proline and positively charged amino acids at their C-terminal, contributing to ACE inhibition.
The present study aimed to evaluate the effects of two different enzymes, one derived from microbial sources and the other from animal sources, on the peptide profile with low molecular weight (<3 kDa) and ACE-inhibitory activity of White (Beyaz) cheese produced from ultrafiltered (UF) milk. The control group's cheeses were produced using pasteurized milk. Throughout the 90-day ripening period, the coagulating enzyme demonstrated no significant effects on the dry matter and protein values (p > 0.05). The protein content of < 3 kDa peptide extracts changed ripening, with no statistically significant effects attributed to the enzyme variation (p > 0.05). ACE inhibition increased in all cheeses by the end of the ripening process (p < 0.05). The ACE-inhibitory activity of < 3 kDa peptide extracts obtained from the UF White cheese produced using the microbial enzyme exhibited an increase corresponding to the observed increase in the total area of RP-HPLC peaks. The LC-MS/MS analysis revealed that the animal-sourced control group yielded the highest number of β-casein and αS1-casein peptides. Many < 3 kDa peptides described in the present possessed proline and positively charged amino acids at their C-terminal, contributing to ACE inhibition.