Abstract

BackgroundSpecific interests in improving the functionality of food proteins as well as in protein‒food constituent interactions have resulted in a tremendous number of scientific papers. However, the fundamental mechanisms on protein structures and dynamics in different environments and conditions remain unknown, which hampers structure-based design of food proteins with predictable properties and desired functionalities. The technical barriers in probing structural basis of food protein functionality is one of the major barriers for such situation. Scope and approachThe aim of this review article is to delineate the ability of site directed spin-labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy to unravel food protein structure and dynamics in atomic levels. The review highlights the importance of food protein structures and dynamics in terms of their functionality in food systems. Detailed applications of SDSL-EPR in deciphering structural and dynamics information of biological proteins are provided. A few key areas that SDSL-EPR can help improve the understanding of the fundamental relationship between structure and functionality of food proteins are proposed. Lastly, the limitations of SDSL-EPR in food systems and the solutions are outlined. Key findings and conclusionsSDSL-EPR offers exceptional advantages to study food protein structure, dynamics, and interactions. The adoption of SDSL-EPR may open up a new horizon on understanding food protein structure and dynamic at an atomic level. Unlike the current trial-and-error methods, the information gained by SDSL-EPR could help food scientist rational design food systems with desirable functionalities based upon the ability to predict how protein structure affects functionality.

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