Excessive free radical grafting interferes with the macromolecular association and crystallization of brined porcine myofibrils during heat-set gelatinization

Min Zhang; Lichao He; Yanbo Wang; Chengliang Li; Yongguo Jin; Guofeng Jin; Xiaoyan Tang

doi:10.1016/j.foodres.2023.113709

Excessive free radical grafting interferes with the macromolecular association and crystallization of brined porcine myofibrils during heat-set gelatinization

Food Res Int. 2024 Jan:175:113709. doi: 10.1016/j.foodres.2023.113709. Epub 2023 Nov 19.

Authors

Min Zhang¹, Lichao He², Yanbo Wang², Chengliang Li³, Yongguo Jin⁴, Guofeng Jin⁵, Xiaoyan Tang⁶

Affiliations

¹ School of Food and Health, Beijing Technology and Business University, Beijing 100048, China; State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China; College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
² School of Food and Health, Beijing Technology and Business University, Beijing 100048, China.
³ School of Food and Health, Beijing Technology and Business University, Beijing 100048, China; College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
⁴ College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
⁵ School of Food and Health, Beijing Technology and Business University, Beijing 100048, China. Electronic address: jinguofeng@btbu.edu.cn.
⁶ Key Laboratory of Agro-Product Quality and Safety, Institute of Quality Standard & Testing Technology for Agro-Products, Chinese Academy of Agricultural Sciences, Beijing 100081, China. Electronic address: txycaas@126.com.

PMID: 38129033
DOI: 10.1016/j.foodres.2023.113709

Abstract

Free radical grafting and oxidative modification show superiority in myofibrillar protein (MP) aggregation patterns during salting process, but their consequent formation mechanisms of protein hydration network require further evaluation. Herein, we explored the effect of salt-curing (0, 1, 3 and 5 %) on MP protein polymer substrate, water-protein interaction, crystallization events and thermal stability under H₂O₂/ascorbate-based hydroxyl radical (•OH)-generating system (HRGS) (1, 10, 20 mM H₂O₂). Results showed that moderate salting (≤3%) favored the water binding of MP gels during the oxidation course. Accordingly, the maximum thermal stability (T_m) of MP gels was obtained at 3 % salting could be greatly attributed to the protein chain solubilization and refolding process. However, 5 % salt synergized with •OH oxidation intensified diffraction peak 2 (the most striking diffraction feature). Microstructural analysis validated a maximum compactness of MP gel following brining with 5 % salt at potent oxidation strength (20 mM H₂O₂). This study maybe promises efficient strategy to the myogenetic fibril products and biomaterials.

Keywords: Crystallization; Free radical grafting; Heat-set gelatinization; Myofibril; Salt diffusion; Thermodynamics.

MeSH terms

Animals
Crystallization
Gels / chemistry
Hot Temperature*
Hydrogen Peroxide / metabolism
Muscle Proteins / chemistry
Myofibrils* / chemistry
Swine
Water / chemistry

Substances

Hydrogen Peroxide
Muscle Proteins
Gels
Water