Study on hypoglycemic and lipid-lowering activity of shrimp shell-derived enzymatic hydrolysate and peptide sequence function analysis

Abstract

Objective: The PCSPHs were prepared by enzymatic hydrolysis of Procambarus clarkii shells, and their hypoglycemic and lipid-lowering activities in vitro were evaluated and peptide sequence were analyzed. Methods: Different crayfish shell proteolysates were prepared by hydrolysis of pepsin, alcalase protease, trypsin, flavor protease and papain, and their in vitro hypoglycemic and lipid-lowering activities were evaluated and peptide sequences were determined. The peptides sequence of Procambarus clarkii shells was identified by LC-MS/MS. Taking the crystal structure of the nuclear receptor PPARγ ligand binding region as the target, Autodock vina was used to simulate molecular docking to obtain crayfish shell peptides with potential hypoglycemic/lipid-lowering activities. Results: The PEP-PCSPHs had significant inhibitory effects on α-amylase and α-glucosidase activity, with IC50 values of （5.42±0.05） mg/mL and （7.11±1.01） mg/mL, respectively. The TRY-PCSPHs had the strongest inhibitory effect on pancreatic lipase activity, with an IC50 of （4.71±1.12） mg/mL, and exhibited the best in vitro binding effects on sodium glycinocholate. In addition, 3 391 peptide sequences were identified in pepsin hydrolysates and 2 086 peptide sequences were identified in trypsin hydrolysates, and multiple hypoglycemic/lipid-lowering crayfish shell active peptides that could bind to PPARγ were screened through online website prediction and molecular docking. Conclusion: The shrimp shell peptides prepared by enzymatic hydrolysis of crayfish shells have potential hypoglycemic and lipid-lowering activities, which may play a role in improving glucose and lipid metabolism disorders.

Keywords

• procambarus clarkii shells
• protein hydrolysate
• pparγ
• molecular docking
• hypoglycemic and lipid-lowering activity