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. 2024 Feb 28;13(5):745.
doi: 10.3390/foods13050745.

Preparation, Structural Identification, and Screening of Egg-Derived Peptides with Facilitating Alcohol Metabolism Activity

Yali Tan  1   2 , Yulin Wang  1 , Yuan Wan  2 , Yu Liang  2 , Qiaocui Liu  2 , Mengya Wei  2 , Tao Hou  1   2   3
Affiliations

Preparation, Structural Identification, and Screening of Egg-Derived Peptides with Facilitating Alcohol Metabolism Activity

Yali Tan et al. Foods. .

Abstract

The aim of this study was to obtain egg-derived peptides with facilitating alcohol metabolism (EPs) by enzymolysis, to identify their structures, and screen small polypeptides with higher activity by molecular docking. The optimum conditions for preparing EPs with facilitating alcohol metabolism were obtained by a single factor experiment, adding 2% Protamex and performing enzymolysis for 3 h with a liquid-material ratio of 35:1. The dose-response relationship experiment showed that 800 mg/kg·bw EPs played a better role in facilitating alcohol metabolism. EPs contained 40% hydrophobic amino acids (HAA), including 9.24% Leu. Eighty-four peptides were identified by HPLC-MS/MS and four peptides with potential activation of alcohol dehydrogenase were further selected by molecular docking. The tetrapeptide Trp-Ile-Val-Asp (WIVD) with the highest binding energy reached -7.16 kcal/mol. These findings suggest that egg is a good source for the preparation of peptides with facilitating alcohol metabolism activity.

Keywords: anti-alcohol activity; egg; molecular docking; structure identification.

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Conflict of interest statement

The authors declare that there are no conflicts interest.

Figures

Figure 1
Figure 1
The effect of different proteases (a,b), liquid–material ratios (c,d), enzyme additive quantities (e,f), enzymatic hydrolysis times (g,h) on the DH, BAC elimination rate, and ADH activation rate. Different letters indicate significant differences (p < 0.05).
Figure 2
Figure 2
The effect of HWJZ and different doses of EPs on the BAC elimination rate (a), liver ADH (b) and ALDH (c) activity, serum AST (d), and ALT (e) activity, liver GSH (f) and MDA (g). Different letters indicate significant differences (p < 0.05).
Figure 3
Figure 3
Total ion flow diagram of EPs.
Figure 4
Figure 4
Docking results visualization of the four lowest binding energy peptides with ADH. WIVD (a), IDNWE (b), KPIE (c), and TPVVD (d).
Figure 5
Figure 5
The EC50 values of ADH activation rates in vitro of different peptides. Different letters indicate significant differences (p < 0.05).
See this image and copyright information in PMC

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