The primary structure identification of a corn peptide facilitating alcohol metabolism by HPLC-MS/MS.

The aim of this study is to identify the primary structure of corn peptides (CPs) with a facilitating alcohol metabolism effect. Corn protein was hydrolyzed by Alcalase first. The hydrolysate, crude corn peptides (CPs), was then fractionated through ultrafiltration technology. The primary structure of a peptide from the fraction (Mm<5kDa) was identified by HPLC-MS/MS, coupled with the peptide sequence retrieval using the MS-MS online database. The amino acid sequence of the peptide was determined as Q-L-L-P-F, and the pentapeptide was synthesized by Fmoc solid-phase peptide synthesis (SPPS) method. Its ability to facilitate alcohol metabolism was evaluated in vivo. Results showed that the synthetic peptide (10mg/kg) had a higher ability to eliminate alcohol in vivo compared to the mixed peptides (Mm<5kDa, 200mg/kg). In conclusion, the pentapeptide Q-L-L-P-F has a potent ability in facilitating alcohol metabolism, and this pentapeptide is the main bioactive component in the mixed peptides obtained from corn.