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

• Published in: Food chemistry Vol. 469; p. 142537
• Main Authors: Zhu, Mingming, Jiang, Lijie, Liu, Wang, Li, Huijie, Jiao, Lingxia, Ma, Hanjun, Gao, Xueli, Kang, Zhuangli
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 30.03.2025
• Subjects: adenosine triphosphate; amino acids; Animals; biomarkers; biosynthesis; denaturation; food chemistry; Food Preservation - instrumentation; Food Preservation - methods; Freezing; Low-frequency alternating magnetic field-assisted freezing; Magnetic Fields; magnetism; Muscle Proteins - chemistry; Muscle Proteins - metabolism; Myofibrils - chemistry; Myofibrils - metabolism; oxidation; Oxidation-Reduction; oxidative phosphorylation; Porcine myofibrillar proteins; pork; Pork Meat - analysis; pork quality; Protein oxidation; Proteomics; Red Meat - analysis; refrigerators; spectral analysis; Structure; Swine; Low-frequency alternating magnetic field-assisted freezing; Protein oxidation; Structure; Porcine myofibrillar proteins; Proteomics
• ISSN: 0308-8146; 1873-7072; 1873-7072
• DOI: 10.1016/j.foodchem.2024.142537

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. [Display omitted] •LF-MFF-4 preserved MPs' structural integrity by mitigating oxidative denaturation.•Identified 126 DAPs linked to key pathways, potentially impacting ATP metabolism.•Correlation analysis and VIP score identified eight proteins as biomarkers for MPs.