Bioactivity of collagen peptides derived from commercial animals: In silico investigation

• DOI: 10.1016/j.lwt.2023.115381
• Publication Date: 2023-10-03T06:33:02Z
• Authors: Yakun Hou; Bimal Chitrakar; Kemin Mao; Ke Wang; Xin Gu; Jie Gao; Qing Zhang; Alaa El-Din Ahmed...; Yaxin Sang
• Keywords: Pepsin; Dipeptidyl peptidase; Oligopeptide

Collagen peptides (CP) obtained from collagen hydrolysis have drawn much attention for their broad bioactivities, such as antioxidant, anti-inflammatory, angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities. This study employed an in silico approach to investigate the bioactivities of CP fish, chicken, cattle, pig, yak, sheep, donkey. BLAST analysis amino acid sequences showed mammals had comparable but those fish chicken possessed different bioactivity potential due low protein homology. In with gastrointestinal enzymes, including trypsin, pepsin, proteinase K that number bioactive (922) (737–905) was higher than (544–675) because lower content proline collagen, amount percentage total generated tilapia highest (86.4%). The most common were ACE DPP-IV A molecular docking Thr-Phe Gly-Phe strongest binding energy enzymes involved DPP-IV, respectively, indicating a good source anti-hypotensive anti-hypoglycaemic peptides.