Heat-induced oxidation and proteomic changes to yak milk protein

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...

وصف كامل

التفاصيل البيبلوغرافية
الحاوية / القاعدة:Food Science of Animal Products
المؤلفون الرئيسيون: Jinchao Zhang, Yu Zhang, Rong Jing, Senbiao Shu, Jie Yang, Liang Li, Wenhan Wang, Zhendong Liu
التنسيق: مقال
اللغة:الإنجليزية
منشور في: Tsinghua University Press 2024-03-01
الموضوعات:
الوصول للمادة أونلاين:https://www.sciopen.com/article/10.26599/FSAP.2024.9240056
_version_ 1849904115139739648
author Jinchao Zhang
Yu Zhang
Rong Jing
Senbiao Shu
Jie Yang
Liang Li
Wenhan Wang
Zhendong Liu
author_facet Jinchao Zhang
Yu Zhang
Rong Jing
Senbiao Shu
Jie Yang
Liang Li
Wenhan Wang
Zhendong Liu
author_sort Jinchao Zhang
collection DOAJ
container_title Food Science of Animal Products
description 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.
format Article
id doaj-art-e66d03f03e4f45fcb8474b8aaa8ecc0c
institution Directory of Open Access Journals
issn 2958-4124
2958-3780
language English
publishDate 2024-03-01
publisher Tsinghua University Press
record_format Article
spelling doaj-art-e66d03f03e4f45fcb8474b8aaa8ecc0c2025-08-20T00:58:04ZengTsinghua University PressFood Science of Animal Products2958-41242958-37802024-03-0121924005610.26599/FSAP.2024.9240056Heat-induced oxidation and proteomic changes to yak milk proteinJinchao Zhang0Yu Zhang1Rong Jing2Senbiao Shu3Jie Yang4Liang Li5Wenhan Wang6Zhendong Liu7Tibet Agriculture & Animal Husbandry University, Nyingchi 860000, ChinaCollege of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, ChinaTibet Agriculture & Animal Husbandry University, Nyingchi 860000, ChinaTibet Agriculture & Animal Husbandry University, Nyingchi 860000, ChinaTibet Agriculture & Animal Husbandry University, Nyingchi 860000, ChinaTibet Agriculture & Animal Husbandry University, Nyingchi 860000, ChinaNational 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, ChinaTibet Agriculture & Animal Husbandry University, Nyingchi 860000, ChinaYak 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.https://www.sciopen.com/article/10.26599/FSAP.2024.9240056yak milkproteinoxidationheat treatmentsproteomicsstructure
spellingShingle Jinchao Zhang
Yu Zhang
Rong Jing
Senbiao Shu
Jie Yang
Liang Li
Wenhan Wang
Zhendong Liu
Heat-induced oxidation and proteomic changes to yak milk protein
yak milk
protein
oxidation
heat treatments
proteomics
structure
title Heat-induced oxidation and proteomic changes to yak milk protein
title_full Heat-induced oxidation and proteomic changes to yak milk protein
title_fullStr Heat-induced oxidation and proteomic changes to yak milk protein
title_full_unstemmed Heat-induced oxidation and proteomic changes to yak milk protein
title_short Heat-induced oxidation and proteomic changes to yak milk protein
title_sort heat induced oxidation and proteomic changes to yak milk protein
topic yak milk
protein
oxidation
heat treatments
proteomics
structure
url https://www.sciopen.com/article/10.26599/FSAP.2024.9240056
work_keys_str_mv AT jinchaozhang heatinducedoxidationandproteomicchangestoyakmilkprotein
AT yuzhang heatinducedoxidationandproteomicchangestoyakmilkprotein
AT rongjing heatinducedoxidationandproteomicchangestoyakmilkprotein
AT senbiaoshu heatinducedoxidationandproteomicchangestoyakmilkprotein
AT jieyang heatinducedoxidationandproteomicchangestoyakmilkprotein
AT liangli heatinducedoxidationandproteomicchangestoyakmilkprotein
AT wenhanwang heatinducedoxidationandproteomicchangestoyakmilkprotein
AT zhendongliu heatinducedoxidationandproteomicchangestoyakmilkprotein