Proteomics-Discovered Quality Biomarkers for Chilled/Frozen Meat and Aquatic Products: Translational Barriers from Lab to Industry and Breakthrough Directions
Main Article Content
Keywords
protein biomarkers, proteomics, chilling/freezing, meat and aquatic products, translational gaps
Abstract
Over the past decade, proteomics has identified numerous differentially abundant proteins and post‑translational modifications in chilled and frozen meat and aquatic products, holding promise as molecular markers for quality monitoring. Yet, these candidates have rarely been used in commercial cold‑chain surveillance or rapid testing. This review asks a more practical question: what prevents proteomic findings from moving into industrial use? To keep the discussion focused, candidate biomarkers are grouped into three types: degradation fragments (e.g. the 30 kDa troponin‑T fragment), oxidized proteins (e.g. carbonylated creatine kinase), and abundance‑changed enzymes/chaperones (e.g. Hsp27/Hsp70). Across the literature, four barriers appear repeatedly: (1) insufficient validation of storage‑condition universality; (2) difficulty migrating quantitative methods from mass spectrometry to rapid detection formats; (3) lack of quantitative models linking biomarker changes to sensory/textural quality indices; and (4) scarcity of cross‑species and cross‑processing stability data. The main purpose of this review is to map where translation breaks down between discovery and application. Rather than treating proteomic identification as an endpoint, it examines the points where potential markers fail to become workable tools for quality monitoring. That gap matters. A candidate may perform well under controlled experimental conditions and still be difficult to apply in routine commercial testing. Based on this, the review organizes a specific set of translational problems and a research agenda that may help move freshness/freeze‑thaw history markers closer to practical cold‑chain quality control in the food industry.
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