Purification and identification of corn peptides that facilitate alcohol metabolism by semi-preparative high-performance liquid chromatography and nano liquid chromatography with electrospray ionization tandem mass spectrometry

In this study, peptides that facilitate alcohol metabolism were purified and identified from corn protein hydrolysates. The ultra‐filtered fraction with a molecular weight < 3 kDa (F3) potential activity was separated into six fractions (F3‐H1–F3‐H6) by semi‐preparative high‐performance liquid ch...

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Bibliographic Details
Published in:Journal of separation science 2016-11, Vol.39 (21), p.4234-4242
Main Authors: Ma, Zhi-Li, Hou, Tao, Shi, Wen, Liu, Wei-Wei, Ibrahim, Salam A., He, Hui
Format: Article
Language:English
Subjects:
Alcohol
Alcohol metabolism
Alcohols
Chromatography
Corn
Corn peptides
High-performance liquid chromatography
Ionization
Ions
Liquid chromatography
Mass spectrometry
Metabolism
Nanostructure
Peptides
Scientific imaging
Structural characterization
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Summary:In this study, peptides that facilitate alcohol metabolism were purified and identified from corn protein hydrolysates. The ultra‐filtered fraction with a molecular weight < 3 kDa (F3) potential activity was separated into six fractions (F3‐H1–F3‐H6) by semi‐preparative high‐performance liquid chromatography. Among the resultant six fractions, F3‐H4 and F3‐H5 exhibited the highest ability to eliminate alcohol in vivo. A total of 16 peptides with strong signal values were identified from F3‐H4 and F3‐H5 fractions by nano liquid chromatography coupled with electrospray ionization tandem mass spectrometry. Several identified peptides were then selected and synthesized to determine their potential to facilitate alcohol metabolism. We found that Leu‐Leu and Pro‐Phe were the key structure units in Gln‐Leu‐Leu‐Pro‐Phe responsible for this peptide's ability to facilitate alcohol metabolism. However, the role of Leu‐Leu and Pro‐Phe may be affected by peptide chain length and hydrophobic properties. Our results have thus provided some insight into the study of the structure–activity relationships of corn peptides.
ISSN:1615-9306
1615-9314
DOI:10.1002/jssc.201600554