A review of physical and chemical protein‐gel induction

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Abstract
Summary Protein gelation is important to obtain desirable sensory and textural structures in foods. Gelation phenomenon requires a driving force to unfold the native protein structure, followed by an aggregation retaining a certain degree of order in the matrix formed by association between protein strands. Protein gelation has been traditionally achieved by heating, but some physical and chemical processes form protein gels in an analogous way to heat‐induction. A physical means, besides heat, is high pressure. Chemical means are acidification, enzymatic cross‐linking, and use of salts and urea, causing modifications in protein–protein and protein–medium interactions. The characteristics of each gel are different and dependent upon factors like protein concentration, degree of denaturation caused by pH, temperature, ionic strength and/or pressure.