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Research Article | Open Access

Heat-induced oxidation and proteomic changes to yak milk protein

Jinchao Zhang1,§, Yu Zhang2,§, Rong Jing1, Senbiao Shu1, Jie Yang1, Liang Li1,3, Wenhan Wang4( ), Zhendong Liu1,3( )
Tibet Agriculture & Animal Husbandry University, Nyingchi 860000, China
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China
The Provincial and Ministerial Co-founded Collaborative Innovation Center for R&D in Tibet Characteristic Agricultural and Animal Husbandry Resources, Tibet Agriculture & Animal Husbandry University, Nyingchi 860000, China
National Engineering Research Center of Edible Fungi, Key Laboratory of Applied Mycological Resources and Utilization of Ministry of Agriculture, Shanghai Key Laboratory of Agricultural Genetics and Breeding; Institute of Edible Fungi, Shanghai Academy of Agricultural Sciences, Shanghai 201403, China

§These authors contributed equally to this work.

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Graphical Abstract

Abstract

Yak milk is a dietary source of high-quality protein in the plateau region of China but as yet uncharacterized oxidative changes occur during heat treatment. Therefore, oxidation of and proteomic changes to milk proteins from plateau pasture-fed yaks after at different temperatures were investigated. Content of carbonyl groups, surface hydrophobicity increased, and total sulfhydryl, disulfide bond content decreased. Endogenous fluorescence intensity decreased after at increasing temperatures, indicating increased particle size, and absolute values of the zeta potential decreased. Analysis by Fourier transform infrared spectroscopy showed changes of the secondary structure, with relative content of α-helices increasing and then decreasing, β-sheet showed a trend of decreasing and then increasing while the relative content of random curl did not change. The close range of the β-turn gradually decreased, breaking the protein microstructure, and folding stacking occurred. Proteomics analyses showed a temperature dependent effect. Sixty-two proteins were suppressed and 49 elevated with 4 pathways up-regulated and 7 down-regulated at 65 °C. Thirty-one proteins were suppressed and 37 elevated with 5 pathways up-regulated and 4 down-regulated at 90 °C. The most extensive changes were observed at 120 °C, when 327 proteins were suppressed and 308 elevated with 11 pathways up-regulated and 33 down-regulated.

Keywords

yak milkproteinoxidationheat treatmentsproteomicsstructure

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Food Science of Animal Products
Volume 2 Issue 1,
March 2024
Article number: 9240056
DOI: 10.26599/FSAP.2024.9240056
Cite this article:
Zhang J, Zhang Y, Jing R, et al. Heat-induced oxidation and proteomic changes to yak milk protein. Food Science of Animal Products, 2024, 2(1): 9240056. https://doi.org/10.26599/FSAP.2024.9240056

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Received: 07 April 2024
Revised: 15 April 2024
Accepted: 07 May 2024
Published: 11 June 2024
© Beijing Academy of Food Sciences 2024.

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/).
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