Analysis of the influencing mechanism of low-frequency alternating magnetic field-assisted freezing on oxidative and structural attributes of pork myofibrillar proteins based on proteomic changes

Mingming Zhu; Lijie Jiang; Wang Liu; Huijie Li; Lingxia Jiao; Hanjun Ma; Xueli Gao; Zhuangli Kang

doi:10.1016/j.foodchem.2024.142537

Analysis of the influencing mechanism of low-frequency alternating magnetic field-assisted freezing on oxidative and structural attributes of pork myofibrillar proteins based on proteomic changes

Food Chem. 2024 Dec 17:469:142537. doi: 10.1016/j.foodchem.2024.142537. Online ahead of print.

Authors

Mingming Zhu¹, Lijie Jiang², Wang Liu², Huijie Li², Lingxia Jiao³, Hanjun Ma², Xueli Gao⁴, Zhuangli Kang⁵

Affiliations

¹ School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; Research and Experimental Base for Traditional Specialty Meat Processing Techniques of the Ministry of Agriculture and Rural Affairs of the People's Republic of China, Xinxiang 453003, China. Electronic address: happyzhumingming@126.com.
² School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China.
³ School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China. Electronic address: jiaolingxia@163.com.
⁴ Food and Pharmacy College, Xuchang University, Xuchang 461000, China.
⁵ School of Tourism and Cuisine, Yangzhou University, Yangzhou 225127, China.

PMID: 39708654
DOI: 10.1016/j.foodchem.2024.142537

Abstract

Using quantitative proteomics, the study investigated the effects of low-frequency alternating magnetic field-assisted freezing (LF-MFF) on the oxidative status and structural integrity of porcine myofibrillar proteins (MPs). LF-MFF, especially at 3 mT (LF-MFF-3) and 4 mT (LF-MFF-4), significantly reduced MPs' oxidation compared to refrigerator freezing (RF) (P < 0.05). The spectroscopic analysis confirmed better structural preservation with LF-MFF-4. We identified 126 differentially abundant proteins (DAPs) associated with key metabolic pathways, including amino acid biosynthesis and oxidative phosphorylation, potentially affecting Adenosine Triphosphate (ATP) metabolism and contributing to freeze-induced protein damage and oxidative denaturation of MPs. Through correlation analysis, among the 52 DAPs in the LF-MFF-4 vs RF comparison, eight proteins with variable importance in projection (VIP) > 1.1 were identified as potential biomarkers for porcine MPs. These findings enhance our understanding of the oxidative and structural changes in MPs following LF-MFF, suggesting its potential for improving pork quality and meat preservation.

Keywords: Low-frequency alternating magnetic field-assisted freezing; Porcine myofibrillar proteins; Protein oxidation; Proteomics; Structure.