Effects of hydroxyl radical oxidation on the stability and biochemical functions of rex rabbit meat

被引:1
作者
Liu, Shuyun [1 ]
Li, Hongjun [1 ,2 ,3 ]
Yang, Li [1 ]
He, Zhifei [1 ,2 ,3 ]
机构
[1] Southwest Univ, Coll Food Sci, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
[2] Chongqing Key Lab Special Food Cobuilt Sichuan & C, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
[3] Chongqing Engn Res Ctr Reg Food, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
关键词
Leporidae; The whole muscle homogenates; Myofibrillar protein; Lipid oxidation; Protein oxidation; LIPID OXIDATION; MYOFIBRILLAR PROTEIN; MYOSIN; MALONDIALDEHYDE; MECHANISMS; MYOGLOBIN; PRODUCTS; CAPACITY; QUALITY; BINDING;
D O I
10.1016/j.lwt.2024.116295
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Reactive oxygen species (ROS)-generating system in muscle food is an important factor as it greatly influences shelf life and quality of meat. In this study, whole muscle homogenate was used as the research object, and the Fenton reaction system as an inducer was established for analyzing the effect of oxidation on Chuanbai Rex and Hyla rabbits meat. The homogenates were exposed to varying concentrations of hydrogen peroxide (H2O2, 0, 2, 4, 6, 8, and 10 mmol/L), the level of lipid oxidation of both breeds increased with the increased H2O2 concentration, while Hyla rabbits was higher. Oxidation and molecular aggregation of myofibrillar protein (MP) was observed in both breeds, including formation of carbonyl compounds, depleted sulphydryl, and increased hydrophobicity while fluorescence decreased. After oxidation, the loss of amino acids was higher in Hyla (16%) than in Rex rabbits (11%). Cys content was identified as the most discriminant parameter capable of elucidating the variations between the two breeds under this oxidation system.
引用
收藏
页数:10
相关论文
共 60 条
  • [1] AMICI A, 1989, J BIOL CHEM, V264, P3341
  • [2] Review: Nutrient density and nutritional value of meat products and non-meat foods high in protein
    Bohrer, Benjamin M.
    [J]. TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2017, 65 : 103 - 112
  • [3] SULFHYDRYL CONTENT OF RABBIT AND TROUT MYOSINS IN RELATION TO PROTEIN STABILITY
    BUTTKUS, H
    [J]. CANADIAN JOURNAL OF BIOCHEMISTRY, 1971, 49 (01): : 97 - &
  • [4] Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein
    Cao, Yungang
    Xiong, Youling L.
    [J]. FOOD CHEMISTRY, 2015, 180 : 235 - 243
  • [5] Technical note:: A simplified procedure for myofibril hydrophobicity determination
    Chelh, Ilham
    Gatellier, Philippe
    Sante-Lhoutellier, Veronique
    [J]. MEAT SCIENCE, 2006, 74 (04) : 681 - 683
  • [6] The role of rabbit meat as functional food
    Dalle Zotte, Antonella
    Szendro, Zsolt
    [J]. MEAT SCIENCE, 2011, 88 (03) : 319 - 331
  • [7] Biochemical changes of Coregonus peled myofibrillar proteins isolates as affected by HRGS oxidation system
    Deng, Xiaorong
    Lei, Yongdong
    Liu, Juan
    Zhang, Jian
    Qin, Junwei
    [J]. JOURNAL OF FOOD BIOCHEMISTRY, 2019, 43 (02)
  • [8] A Comprehensive Review on Lipid Oxidation in Meat and Meat Products
    Dominguez, Ruben
    Pateiro, Mirian
    Gagaoua, Mohammed
    Barba, Francisco J.
    Zhang, Wangang
    Lorenzo, Jose M.
    [J]. ANTIOXIDANTS, 2019, 8 (10)
  • [9] Oxidation of myofibrillar proteins induced by peroxyl radicals: Role of oxidizable amino acids
    Dorta, E.
    Avila, F.
    Fuentes-Lemus, E.
    Fuentealba, D.
    Lopez-Alarcon, C.
    [J]. FOOD RESEARCH INTERNATIONAL, 2019, 126
  • [10] Investigation of the effect of oxidation on the structure of β-lactoglobulin by high resolution mass spectrometry
    Du, Peng-cheng
    Tu, Zong-cai
    Wang, Hui
    Hu, Yue-ming
    Zhang, Jing-jing
    Zhong, Bi-zhen
    [J]. FOOD CHEMISTRY, 2021, 339