High performance liquid chromatography (HPLC) fingerprints and primary structure identification of corn peptides by HPLC-diode array detection and HPLC-electrospray ionization tandem mass spectrometry

• Published in: Yàowu shi͡p︡in fenxi Vol. 24; no. 1; pp. 95 - 104
• Main Authors: Wang, Chi, He, Hui, Zhang, Jiu-liang, Li, Xing, Ma, Zhi-li
• Format: Journal Article
• Language: English
• Published: China (Republic : 1949- ) Elsevier B.V 01.01.2016; Food and Drug Administration; Taiwan Food and Drug Administration
• Subjects: Alcohols; Amino acid sequence; Amino acids; Biological activity; Chromatography; Corn; corn peptides; electrospray ionization mass spectrometry (ESI-MS); Electrospraying; Fingerprinting; Free radicals; Glutamine; High performance liquid chromatography; high-performance liquid chromatography (HPLC); HPLC fingerprints; Identification; Ionization; Lipid peroxidation; Liquid chromatography; Mass spectrometry; Mass spectroscopy; Metabolism; Original; Peptides; Peroxidation; Physiology; primary structure; Proteins; Quality control; Raw materials; Scientific imaging; Spectroscopy; United States > US; China; corn peptides; HPLC fingerprints; electrospray ionization mass spectrometry (ESI-MS); high-performance liquid chromatography (HPLC); primary structure
• ISSN: 1021-9498; 2224-6614
• DOI: 10.1016/j.jfda.2015.05.005

Corn peptides (CPs) are reported to have many biological functions, such as facilitating alcohol metabolism, antioxidation, antitumor, antihypertension, and hepatoprotection. To develop a method for quality control, the high-performance liquid chromatography (HPLC) system was applied. Twenty-eight common peaks were found in all the CPs of corn samples from Enshi, China, based on which, a fingerprinting chromatogram was established for use in quality control in future research. Subsequently, the major chemical constituents of these common peaks were identified respectively using the HPLC-diode-array detection electrospray ionization tandem mass spectrometry (DAD-ESI-MS/MS) system, and 48 peptide fractions were determined ultimately. This was the first time for the majority of these peptides to be reported, and many of them contained amino acids of glutamine (Q), L and A, which might play an important role in the exhibition of the bioactivities of CPs. Many peptides had a similar primary structure to the peptides which had been proven to be bioactive such as facilitating alcohol metabolism, scavenging free radicals, and inhibiting lipid peroxidation. This systematical analysis of the primary structure of CPs facilitated subsequent studies on the relationship between the structures and functions, and could accelerate holistic research on CPs.