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• Bioengineering •     Next Articles

Study on bioactivity of Monascus cheese and screening of ACE inhibitory peptides

2, 2,Zhen MinLIU 2,2, 2,2   

  • Received:2023-08-30 Revised:2024-01-30 Online:2024-03-15 Published:2024-03-29
  • Contact: Zhen MinLIU E-mail:liuzhenmin@brightdairy.com

Abstract: This study investigates the impact of Monascus on bioactive peptides, particularly angiotensin-converting enzyme (ACE) inhibitory peptides during cheese maturation. The contents of soluble nitrogen, the inhibitory activities of α-glucosidase and angiotensin-converting enzyme (ACE) during the ripening process were investigated with cheese without Monascus as the control group. The peptide profile of Monascus cheese was identified. The potential active peptides were screened by bioinformatics and molecular docking, and the screened peptides were synthesized and evaluated. The results showed that compared with the control group, soluble nitrogen content of pH4.6 and trichloroacetic acid (TCA) increased by 57.98% and 38.34%, and α-glucosidase inhibitory activity and ACE inhibitory activity increased by 32.20% and 73.96%, respectively. A total of 1796 peptides were identified in the extract of Monascus cheese, including 51 ACE inhibitory peptides, 28 antioxidant peptides and 7 glucose-lowering peptides. Two ACE inhibitory peptides YPFPGPI and FPEVFGK were screened, and the IC50 values were 125.53 and 285.73 μmol/L, respectively. The enzyme inhibition types were non-competitive inhibition. This study provides a rapid screening method for ACE inhibitory peptides, and proves that the addition of Monascus in cheese can effectively improve the ACE inhibitory activity, which provides a reference for exploring the potential of functional properties of Monascus cheese.

Key words: Monascus, cheese, angiotensin-converting enzyme, bioinformatics, molecular docking, enzyme inhibition kinetics