Oxidative mechanism of chicken wooden breast myofibrillar protein

被引:0
作者
Wang, Ke [1 ,2 ]
Zhang, Yimin [2 ]
Sun, Jingxin [1 ,3 ]
机构
[1] Qingdao Agr Univ, Coll Food Sci & Engn, Qingdao 266109, Peoples R China
[2] Shandong Agr Univ, Coll Food Sci & Engn, Tai An 271018, Peoples R China
[3] Qingdao Agr Univ, Shandong Res Ctr Meat Food Qual Control, Qingdao 266109, Peoples R China
关键词
Wooden breast; Myofibrillar protein; Free radical; Oxidation; Physicochemical property; Molecular structure; MUSCLE; MEAT;
D O I
10.26599/FSHW.2023.9250026
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
To explore the oxidation mechanism of wooden breast myofibrillar protein (WBMP), oxidative breast MP (OBMP) was obtained from different doses (3, 10, and 20 mmol/L) of H2O2 oxidized normal breast MP (NBMP). The results showed that the Zeta-potential, particle size, solubility, sulfhydryl, and carbonyl contents of OBMP-3 (3 mmol/L, low-dose free radicals) and WBMP were similar. Fluorescence spectrum analysis showed that the oxidation of low-dose free radicals led to a significant increase in the surface hydrophobicity (from 214.03 +/- 10.03 to 393.50 +/- 10.33) and tryptophan fluorescence intensity (from 185.71 to 568.32). In addition, the alpha-helix content of WBMP decreased significantly from (37.46 +/- 1.15)% (NBMP) to (34.70 +/- 2.04)%, while beta-sheet and random coil contents increased significantly (P < 0.05) from (14.37 +/- 0.69)% and (22.24 +/- 0.78)% (NBMP) to (17.70 +/- 0.87)% and (25.20 +/- 1.47)% (WBMP). In summary, low-dose free radical oxidation attacks protein groups, inducing secondary and tertiary structural changes, leading to the formation of WBMP. This work will provide a theoretical basis at the molecular level for exploring the mechanism of functional degradation of WBMP. (c) 2024 Beijing Academy of Food Sciences. Publishing services 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/).
引用
收藏
页码:3415 / 3423
页数:9
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