Fresh pork quality during refrigerated transport and storage may see a significant boost thanks to a novel application of electrostatic fields (EF). Researchers have demonstrated that combining an EF with controlled freezing-point storage can slow the biochemical processes that lead to meat deterioration, offering a potential new method for maintaining freshness without freezing the product.
Postmortem glycolysis, the conversion of muscle glycogen into lactate, is a primary driver of quality loss in fresh meat. As lactate accumulates, pH drops, leading to pale, soft, and exudative meat with poor water-holding capacity. Traditional refrigeration slows this process, but storage near the freezing point provides better preservation, albeit with a need for precise temperature control. Electrostatic-field technology has previously shown promise in improving water distribution and expanding the usable near-freezing temperature range, but its effects on metabolic pathways and enzyme regulation were not well understood.
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 published in Food Quality and Safety (DOI: 10.1093/fqsafe/fyag047) on June 2, 2026. They examined pork muscle stored 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 changes in energy metabolites, glycolytic enzymes, and sarcoplasmic protein structure over 120 hours postmortem.
At the end of the storage period, pork treated with the electrostatic field contained 17.5% less lactate than conventionally refrigerated samples. Glycogen and ATP consumption were 14.9% and 37.3% lower, respectively. The treated samples also retained more pyruvate and exhibited lower Na⁺/K⁺-ATPase activity. Early exposure to the EF promoted larger protein aggregates, but from 36 to 120 hours, proteins became smaller, more dispersed, and more ordered. Enzyme modifications changed with storage time, with the treatment generally reducing phosphorylation and increasing acetylation, consistent with slower glycolytic activity. Correlation analysis linked protein structural shifts with enzyme modification levels.
The authors noted that the preservation effect is not simply due to lower temperature. Instead, the EF appears to influence the molecular environment of glycolytic enzymes, altering protein conformation and the chemical switches that regulate enzyme activity. The time-dependent response is particularly important: proteins initially unfolded and aggregated, then became more dispersed and structurally ordered during prolonged treatment. This sequence may explain the slower conversion of pyruvate into lactate and the better retention of cellular energy.
These 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 could help protect water-holding capacity, texture, appearance, and overall saleable quality during processing, transport, and retail display. The low-power 30-watt system also suggests potential for energy-efficient preservation, though commercial benefits were not directly tested. Future research should validate the proposed causal link between protein structural changes and enzyme post-translational modifications, including 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.
