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.

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Natural carotenoids are an alternative to synthetic orange-red pigments. They are present in crustaceans as a protein-pigment complex. In order to extract this highly unstable pigment, crustacean waste must be stabilized; lactic fermentation is a simple and environmentally friendly method to achieve this goal. Shrimp wastes were inoculated with Lactobacillus bacterial cultures. Carotenoids were then extracted with an organic solvent system. Protein-pigment splitting was carried out using a mixture of 4 commercial enzymes; and the protein was separated from the pigment by ultrafiltration. Electrophoretograms showed that the pigment was attached to a 265-kDa protein. Splitting the protein-pigment complex allows studies on pigment absorption, stability and application.

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