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Abstract
Proteins occur as natural and engineered assemblies in foods. This paper focuses on the microstructural aspects of some protein assemblies and their relation to processing and functionality. Examples discussed include: (a) disassembly of protein bodies in seeds during aqueous extraction; (b) freeze‐texturization and gelation of muscle proteins; (c) formation of large protein aggregates during caking of fish hydrolysate powders; (d) transformation of globular to fibrous aggregates and the role of Tg during extrusion cooking; (e) formation of mixed and filled dairy gels; and (f) kinetics of aggregation of β‐lactoglobulin.