Differences in proteomic and peptide profiles of whey protein by acid curd and enzyme curd process from bovine milk

He Li; Zheng Li; Ying Ma

doi:10.26599/FSAP.2023.9240017

Food Science of Animal Products 2023, 1(2): 9240017 https://doi.org/10.26599/FSAP.2023.9240017

Research Article |

Open Access | Issue | Published: 03 July 2023

Differences in proteomic and peptide profiles of whey protein by acid curd and enzyme curd process from bovine milk

Show Author's Information Hide Author's Information He Li^{¹^,²}, Zheng Li^², Ying Ma^¹(

)

1School of Medicine and Health, Harbin Institute of Technology, Harbin 150090, China

2Jiangsu Engineering Research Center of Cardiovascular Drugs Targeting Endothelial Cells, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China

Keywords:

peptide, whey protein, proteomic, active ingredient

Cite this article:

Li H, Li Z, Ma Y. Differences in proteomic and peptide profiles of whey protein by acid curd and enzyme curd process from bovine milk. Food Science of Animal Products, 2023, 1(2): 9240017. https://doi.org/10.26599/FSAP.2023.9240017

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Abstract

Whey protein, an essential component of milk, possesses a rich repertoire of bioactive proteins with unique nutritional and functional properties. Employing liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS), we conducted a comparative analysis of whey proteins derived from enzyme curd Esprion300HS (E300HS) and acid curd Textrion PROGEL 800 (TP800) methods. Our investigation identified 216 proteins, of which 32 exhibited differential expression between E300HS and TP800. Notably, E300HS displayed significantly higher levels of calcium-binding protein, lactoperoxidase, and lactadherin compared to TP800. Peptide profiling revealed 162 peptides, with 12 upregulated and 14 downregulated in E300HS relative to TP800. Furthermore, E300HS exhibited abundant lactoferrin-derived peptides, while TP800 displayed a higher prevalence of casein-like peptides. These proteins and peptides encompass a broad range of biological functions, including anticancer, antimicrobial, and bone remodeling activities. Our findings underscore the vast potential of whey protein in food industry applications and its significance in cancer research, bone development, and age-related degenerative diseases.

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Differences in proteomic and peptide profiles of whey protein by acid curd and enzyme curd process from bovine milk

Show Author's information Hide Author's Information He Li^{¹^,²}, Zheng Li^², Ying Ma^¹(

)

1School of Medicine and Health, Harbin Institute of Technology, Harbin 150090, China

2Jiangsu Engineering Research Center of Cardiovascular Drugs Targeting Endothelial Cells, School of Life Sciences, Jiangsu Normal University, Xuzhou 221116, China

Abstract

Keywords: peptide, whey protein, proteomic, active ingredient

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Received: 15 March 2023

Revised: 18 May 2023

Accepted: 25 May 2023

Published: 03 July 2023

Issue date: June 2023

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Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).