<p>This study aimed to evaluate the effect of hydrogen-rich water (HRW) supplementation to goats on the ACE inhibitory activity and bioactive peptide of colostrum and mature milk and the potential use of HRW goat milk protein hydrolysates as an effective source of angiotensin-converting enzyme inhibitory (ACE-i) peptides. A total of 31 peptide sequences with potential biological activity were identified in various fragments of caseins and/or whey proteins, including ĸ-CN, αs<sub>2</sub>-CN, β-CN, α-LA, and β-LG. Fragments derived from β-casein with f127-134 (PKYPVEPF), α-LA f43-50 (PEWVCTAF), and β-LG f58-64 (RVYVEEL) were only detected in HRW-supplemented goat milk. The highest formation of free amino acids was observed in HRW-supplemented goat milk samples. Some hydrophilic (Glu, Asn, Ser, Gly, Arg) and hydrophobic (Ala and Pro) amino acids were higher in HRW-supplemented goat milk. ACE-i activity was observed in all samples with a range of 79.30-83.05%. The lowest IC<sub>50</sub> value of milk was 51.68&#xa0;µg mL<sup>− 1</sup> (81.21% ACE inhibitory activity) for HRW-fed goat milk on day 14. Results show that HRW positively affects the composition of free amino acids in goat milk, and, accordingly, the formation of peptides in different sequences with potential ACE-i activity.</p>

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Supplementation of hydrogen-rich water to goats modifies the ACE inhibitory activity and bioactive peptide profile detected by LC–MS–MS of colostrum and mature milk

  • Didem Şahingil,
  • Hilal Kanmaz,
  • Ali Adnan Hayaloğlu,
  • Mushap Kuru,
  • Buket Boğa Kuru,
  • Fikret Bektaşoğlu,
  • Mustafa Makav,
  • Menekşe Bulut,
  • Duried Alwazeer

摘要

This study aimed to evaluate the effect of hydrogen-rich water (HRW) supplementation to goats on the ACE inhibitory activity and bioactive peptide of colostrum and mature milk and the potential use of HRW goat milk protein hydrolysates as an effective source of angiotensin-converting enzyme inhibitory (ACE-i) peptides. A total of 31 peptide sequences with potential biological activity were identified in various fragments of caseins and/or whey proteins, including ĸ-CN, αs2-CN, β-CN, α-LA, and β-LG. Fragments derived from β-casein with f127-134 (PKYPVEPF), α-LA f43-50 (PEWVCTAF), and β-LG f58-64 (RVYVEEL) were only detected in HRW-supplemented goat milk. The highest formation of free amino acids was observed in HRW-supplemented goat milk samples. Some hydrophilic (Glu, Asn, Ser, Gly, Arg) and hydrophobic (Ala and Pro) amino acids were higher in HRW-supplemented goat milk. ACE-i activity was observed in all samples with a range of 79.30-83.05%. The lowest IC50 value of milk was 51.68 µg mL− 1 (81.21% ACE inhibitory activity) for HRW-fed goat milk on day 14. Results show that HRW positively affects the composition of free amino acids in goat milk, and, accordingly, the formation of peptides in different sequences with potential ACE-i activity.