Fresh pork begins to deteriorate almost immediately after slaughter as muscle tissue consumes its remaining energy reserves, leading to quality loss during distribution. Researchers have now demonstrated that applying an electrostatic field (EF) during near-freezing storage can biochemically slow this process, potentially offering a new method to maintain meat quality. The study, published in Food Quality and Safety on June 2, 2026, showed that the treatment preserved more glycogen and adenosine triphosphate (ATP), limited lactate accumulation, and altered the structure of soluble muscle proteins, as well as the post-translational modifications (PTMs) on enzymes that drive glycolysis.
Postmortem glycolysis is a major factor in meat quality deterioration. In this process, muscle glycogen is converted into lactate, which accumulates and causes pH to drop, increasing the risk of pale, soft, and exudative meat with poor water-holding capacity. Conventional refrigeration slows this deterioration, but storage close to the freezing point can provide better preservation, albeit with the need for precise temperature control. Electrostatic-field technology has previously shown promise in improving water distribution and widening the usable near-freezing temperature range, yet its effects on metabolic pathways and enzyme regulation have remained unclear.
Researchers from the Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, and the College of Food Science and Engineering, Ocean University of China, conducted a study to address this gap. They collected longissimus thoracis et lumborum muscle from eight pig carcasses and stored samples under three conditions: conventional refrigeration at 4 ± 0.5 °C, controlled freezing-point storage at −1 ± 0.5 °C, and the same near-freezing conditions with a continuous 12-kilovolt EF. The team tracked samples from 1.5 to 120 hours postmortem, measuring glycogen, glucose, pyruvate, lactate, ATP, and Na⁺/K⁺-ATPase activity. They also quantified phosphorylation and acetylation of key glycolytic enzymes—lactate dehydrogenase (LDH), triosephosphate isomerase (TPI), and pyruvate kinase (PK)—and assessed sarcoplasmic protein structure through particle size, zeta potential, surface hydrophobicity, fluorescence, and secondary structure.
At 120 hours, the electrostatic-field-treated pork contained 17.5% less lactate than conventionally refrigerated samples, while glycogen and ATP consumption were about 14.9% and 37.3% lower, respectively. The treated samples also retained more pyruvate and showed lower Na⁺/K⁺-ATPase activity. Early exposure promoted larger protein aggregates, but from 36 to 120 hours, the proteins became smaller, more dispersed, and more ordered. Enzyme modifications changed with storage time; overall, the treatment tended to reduce phosphorylation and increase acetylation, consistent with slower glycolytic activity. Correlation analysis further connected protein structural shifts with enzyme modification levels.
The authors emphasized that the preservation effect is not simply a consequence of keeping pork colder. Instead, the EF appears to influence the molecular environment in which glycolytic enzymes operate, changing both protein conformation and the chemical switches that regulate enzyme activity. The time-dependent response is especially important: proteins initially unfolded and aggregated, then became more dispersed and structurally ordered during prolonged treatment. This sequence offers a possible explanation for the slower conversion of pyruvate into lactate and better retention of cellular energy during storage.
The findings provide a mechanistic foundation for developing electrostatic-field-assisted cold storage for fresh meat supply chains. By slowing pH decline and conserving ATP, the technology may help protect water-holding capacity, texture, appearance, and saleable quality during processing, transport, and retail display. Its low-power 30-watt system also suggests potential for energy-conscious preservation, although commercial benefits were not directly tested in this experiment. Future work should validate the proposed causal link between protein structural changes and enzyme PTMs, including through molecular dynamics simulations. Larger studies should also assess microbial safety, sensory quality, shelf life, equipment scale-up, temperature fluctuations, operating costs, and performance across different muscles and meat products before industrial adoption.
