Molten globule-state protein structure: Perspectives from food processing applications

Abstract

Under specific pretreatment or processing conditions, spheroprotein can be transformed into a molten globule state, a typical protein conformation with enhanced functionality. Analyzing the correlation between the formation of molten-globule structures and their quality and functional characteristics is critical for developing tailored processing features, especially for minimally processed future foods. This review outlines the mechanisms driving the formation of molten globule proteins through various processes including ultra-high pressure pretreatments, heating, ultrasonication, pH-shifting, macromolecular crowding and exposure to small-molecule denaturants. These treatments yield proteins that retain structural compactness and primary and secondary structures of their native forms, but with modified conformations and increased hydrophobicity. Common methods for characterizing molten globule proteins include fluorescence spectroscopy, circular dichroism spectroscopy, and nuclear magnetic resonance. The review also explores the application of molten globule proteins in food processing, highlighting their potential significance in advancing the field. The detailed elucidation and exploration of the microstructural transition and conformational features of molten globule proteins, together with their quantitative relationship with processibility of proteins from various sources, holds significant implications for optimizing protein-based food processing techniques and achieving targeted improvements in food quality.