Hypolipidemic effects of protein hydrolysates from Trachinotus ovatus and identification of peptides implied in bile acid-binding activity using LC-ESI-Q-TOF-MS/MS.

In the present work, analysis of the hypolipidemic properties of Trachinotus ovatus protein hydrolysates (TOPHs) and identification of peptides with bile acid-binding activity were performed. Hydrolysates prepared by trypsin digestion exhibited the highest in vitro bile acid-binding capacities compared with hydrolysates prepared with the other four proteases and were mainly composed of small peptides and amino acids with molecular weights <3 kDa, accounting for 77.30%. Among the five ultra-filtration fractions of TOPHs, TOPHs-5 (<3 kDa) exhibited the highest in vitro bile acid-binding capacity, which was equivalent to 77.97% of cholestyramine at the same concentration. A total of 68 peptides were identified from TOPHs-5 by LC-ESI-Q-TOF-MS/MS and 9 of them had hydrophobicity of more than 60%. These highly hydrophobic peptides might be associated with the bile acid-binding activity of TOPHs-5. In vivo experiments indicated that the TOPHs could effectively reduce total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C) and the atherogenic index (AI), while they could evidently increase the high-density lipoprotein cholesterol (HDL-C) content. Furthermore, TOPHs exerted a marked protective effect on hepatorenal function, as evidenced by decreased levels of aspartate aminotransferase (AST), alanine aminotransferase (ALT) and creatinine (CREA). Histopathological studies confirmed that TOPHs evidently protected the liver from histological alterations. In summary, for the first time, hypolipidemic effects and subsequential identification were obtained from TOPHs, which are promising natural ingredients that could potentially be employed in the management of hyperlipidemia.