Characterization of structural features of food molten‐globule state proteins: An overview

Abstract During food processing, pH, ionic strength, and temperature drive conformational transitions from native states to partially folded intermediates and fully unfolded states. The molten‐globule (MG) state typically preserves substantial secondary structure but has relaxed tertiary packing, thereby modulating protein solubility, emulsifying activity, gelation, and ligand binding. This review summarizes established approaches for MG‐state characterization, including far‐ and near‐UV CD, FT‐IR, Raman, UV absorption/second‐derivative spectroscopy, intrinsic fluorescence, ANS fluorescence, and NMR spectroscopy, and highlights emerging complementary tools such as HDX‐MS, SAXS, and SPR. Particular attention is given to how moderate hydrophobic exposure, increased conformational flexibility, and restrained aggregation underlie changes in emulsification, foaming, gelation, and binding functionality. This review provides practical guidance for cross‐method interpretation and reproducible characterization of protein conformational states under processing‐relevant conditions.