PDF (3.5 MB)
Collect
Submit Manuscript
Research Article | Open Access

Antioxidant peptides from shrimp by-products: preparation, identification and protective function on H2O2-induced HepG2 cell

Yujie Li1,2Huan Xiang2,3()Shuxian Hao2,3()Hui Huang2,3Shengjun Chen2,3Yongqiang Zhao2,3Di Wang2,3Yueqi Wang2,3Xiaoshan Long2,3
College of Food Science and Engineering, Ocean University of China, Qingdao 266000, China
Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China
Key Laboratory of Efficient Utilization and Processing of Marine Fishery Resources of Hainan Province, Sanya Tropical Fisheries Research Institute, Sanya 572018, China
Show Author Information

Graphical Abstract

View original image Download original image

Abstract

The objective of this study is to identify the antioxidant peptides from shrimp by-products and clarify the underlying protective mechanism involved in HepG2 cells with oxidative stress induced by H2O2. Protein from shrimp by-products was hydrolyzed by three enzymes (neutral protase, alcalase, and Protamex) and the hydrolysates were separated by using Sephadex G-15 gel filtration, among which the A3 (fraction of alcalase-hydrolysate) displayed a significant 1,1-diphenyl-2-picrylhydrazyl radical and 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) cation radical scavenging ability. A total of 3 480 peptides were identified through nano-high performance liquid chromatography-tandem mass spectrometry, with the prediction of five discovered antioxidant peptides (DYPLVPPYF, HFVPVYEGF, GFPPFTGGPFR, EGYPFNPLL, and RVSDGPWLGR). Notably, HFVPVYEGF and EGYPFNPLL emerged as the potent antioxidant peptide, displaying lower half maximal inhibitory concentration. Furthermore, HFVPVYEGF and EGYPFNPLL obviously relieved oxidative stress in HepG2 cells, which strengthened the activity of total-antioxidant capocity, catalase, glutathione peroxidase, and superoxide dismutase, with diminishing the intensity of malondialdehyde and intracellular reactive oxygen species. Molecular docking results revel that HFVPVYEGF and EGYPFNPLL can bind to Kelch-like ECH-associated protein 1 with hydrophobic interactions. The results provided theoretical basis for the production and application of the by-product of shrimp. And a further study should be carried out to examine the bioavailability and in vivo activity of HFVPVYEGF and EGYPFNPLL which identified from shrimp by-products.

References

[1]

M. K. Sivasubramanian, R. Monteiro, M. Jagadeesh, et al., Subramanian, palmitic acid induces oxidative stress and senescence in human brainstem astrocytes, downregulating glutamate reuptake transporters-implications for obesity-related sympathoexcitation, Nutrients 16 (2024) 2852. https://doi.org/10.3390/nu16172852.

[2]
M. Schieber, N. S. Chandel, ROS function in redox signaling and oxidative stress, Curr. Biol. 24 (2014) R453–R462. https://doi.org/10.1016/j.cub.2014.03.034.
[3]
Z. Zhou, J. Han, P. Lang, et al., ROS-responsive self-assembly nanoplatform overcomes hypoxia for enhanced photodynamic therapy, Biomater. Sci. 19 (2024) 5105–5114. https://doi.org/10.1039/D4BM00712C.
[4]

B. Halliwell, Understanding mechanisms of antioxidant action in health and disease, Nat. Rev. Mol. Cell Biol. 25 (2024) 13–33. https://doi.org/10.1038/s41580-023-00645-4.

[5]

S. A. Cunha, M. E. Pintado, Bioactive peptides derived from marine sources: biological and functional properties, Trends Food Sci. Technol. 119 (2022) 348–370. https://doi.org/10.1016/j.jpgs.2021.08.017.

[6]

M. Y. Arancibia, A. Alemán, M. M. Calvo, et al., Antimicrobial and antioxidant chitosan solutions enriched with active shrimp ( Litopenaeus vannamei) waste materials, Food Hydrocoll. 35 (2014) 710–717. https://doi.org/10.1016/j.foodhyd.2013.08.026.

[7]

M. Nikoo, X. Xu, J. M. Regenstein, et al., Autolysis of Pacific white shrimp ( Litopenaeus vannamei) processing by-products: enzymatic activities, lipid and protein oxidation, and antioxidant activity of hydrolysates, Food Biosci. 39 (2021) 100844. https://doi.org/10.1016/j.fbio.2020.100844.

[8]

N. de Los Ángeles Pereira, M. F. Fangio, Y. E. Rodriguez, et al., Characterization of liquid protein hydrolysates shrimp industry waste: analysis of antioxidant and microbiological activity, and shelf life of final product, J. Food Process. Pres. 46 (2022) e15526. https://doi.org/10.1111/jfpp.15526.

[9]

X. Hu, J. Liu, J. Li, et al., Preparation, purification, and identification of novel antioxidant peptides derived from Gracilariopsis lemaneiformis protein hydrolysates, Front. Nutr. 9 (2022) 971419. https://doi.org/10.3389/fnut.2022.971419.

[10]

M. Zhang, L. Zhu, G. Wu, et al., Rapid screening of novel dipeptidyl peptidase-4 inhibitory peptides from pea ( Pisum sativum L.) protein using peptidomics and molecular docking, J. Agric. Food Chem. 70 (2022) 10221–10228. https://doi.org/10.1021/acs.jafc.2c03949.

[11]
P. Zhou, B. Jin, H. Li, et al., HPEPDOCK: a web server for blind peptide-protein docking based on a hierarchical algorithm, Nucleic. Acids Res. 46 (2018) W443–W450. https://doi.org/10.1093/nar/gky357.
[12]

X. Long, X. Hu, C. Pan, et al., Antioxidant activity of Gracilaria lemaneiformis polysaccharide degradation based on Nrf-2/Keap-1 signaling pathway in HepG2 cells with oxidative stress induced by H2O2, Mar. Drugs 20 (2022) 545. https://doi.org/10.3390/md20090545.

[13]

D. Yu, Y. Zha, Z. Zhong, et al., Improved detection of reactive oxygen species by DCFH-DA: new insight into self-amplification of fluorescence signal by light irradiation, Sensor. Actuat. B: Chem. 339 (2021) 129878. https://doi.org/10.1016/j.snb.2021.129878.

[14]

P. J. García-Moreno, I. Batista, C. Pires, et al., Antioxidant activity of protein hydrolysates obtained from discarded Mediterranean fish species, Food Res. Int. 65 (2014) 469–476. https://doi.org/10.1016/j.foodres.2014.03.061.

[15]

K. Zhu, Z. Zheng, Z. Dai, Identification of antifreeze peptides in shrimp byproducts autolysate using peptidomics and bioinformatics, Food Chem. 383 (2022) 132568. https://doi.org/10.1016/j.foodchem.2022.132568.

[16]

A. Jakubczyk, M. Karaś, K. Rybczyńska-Tkaczyk, et al., Current trends of bioactive peptides-new sources and therapeutic effect, Foods 9 (2020) 846. https://doi.org/10.3390/foods9070846.

[17]

T. H. Olsen, B. Yesiltas, F. I. Marin, et al., AnOxPePred: using deep learning for the prediction of antioxidative properties of peptides, Sci. Rep. 10 (2020) 21471. https://doi.org/10.1038/s41598-020-78319-w.

[18]

Z. Hu, C. Liu, C. Niu, et al., Identification and virtual screening of novel antioxidant peptides from brewing by-products and their cytoprotective effects against H2O2-induced oxidative stress, Food Biosci. 58 (2024) 103686. https://doi.org/10.1016/j.fbio.2024.103686.

[19]

J. E. Aguilar-Toalá, A. M. Liceaga, Cellular antioxidant effect of bioactive peptides and molecular mechanisms underlying: beyond chemical properties, Int. J. Food Sci. Technol. 56 (2021) 2193–2204. https://doi.org/10.1111/ijfs.14855.

[20]

Y. Ren, G. Zheng, L. You, et al., Structural characterization and macrophage immunomodulatory activity of a polysaccharide isolated from Gracilaria lemaneiformis, J. Funct. Foods 33 (2017) 286–296. https://doi.org/10.1016/j.jff.2017.03.062.

[21]

Q. J. Yan, L. H. Huang, Q. Sun, et al., Isolation, identification and synthesis of four novel antioxidant peptides from rice residue protein hydrolyzed by multiple proteases, Food Chem. 179 (2015) 290–295. https://doi.org/10.1016/j.foodchem.2015.01.137.

[22]

J. Wang, G. Wang, Y. Zhang, et al., Novel angiotensin-converting enzyme inhibitory peptides identified from walnut glutelin-1 hydrolysates: molecular interaction, stability, and antihypertensive effects, Nutrients 14 (2021) 151. https://doi.org/10.3390/nu14010151.

[23]

L. Baird, M. Yamamoto, The molecular mechanisms regulating the KEAP1-NRF2 pathway, Mol. Cell Biol. 40 (2020) e00099-20. https://doi.org/10.1128/MCB.00099-20.

[24]

A. V. Ulasov, A. A. Rosenkranz, G. P. Georgiev, et al., Nrf2/Keap1/ARE signaling: towards specific regulation, Life Sci. 291 (2022) 120111. https://doi.org/10.1016/j.lfs.2021.120111.

[25]

Y. Zhang, Y. Liu, W. Li, et al., Antioxidant activity of soybean peptides and Keap1 protein: a combined in vitro and in silico analysis, LWT-Food Sci. Technol. 212 (2024) 117019. https://doi.org/10.1016/j.lwt.2024.117019.

Food Science of Animal Products
Article number: 9240100
Cite this article:
Li Y, Xiang H, Hao S, et al. Antioxidant peptides from shrimp by-products: preparation, identification and protective function on H2O2-induced HepG2 cell. Food Science of Animal Products, 2025, 3(1): 9240100. https://doi.org/10.26599/FSAP.2025.9240100
Metrics & Citations  
Article History
Copyright
Rights and Permissions
Return