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Protein Digestibility: In Vitro Methods of Assessment

1991; Elsevier BV; Linguagem: Inglês

10.1016/s1043-4526(08)60065-0

2213-6797

Harold E. Swaisgood, George L. Catignani,

Protein Hydrolysis and Bioactive Peptides

This chapter describes those changes in protein structure that lead to change in the digestibility of the protein and discusses several methods for assaying protein digestibility The biological utilization of a protein is primarily dependent on its digestibility by gastric, pancreatic, and intestinal peptidases; its composition, particularly with respect to the essential amino acids; and the absorption or transport of amino acids and di- and tri-peptides into the blood. In vitro methods plays an important role in assaying protein digestibility, because these methods are more rapid, simple, and potentially could be used commercially for monitoring protein quality. Modifications that commonly affect protein digestibility include proteolysis, thermal unfolding, aggregation, carbonyl-amine reactions, racemization, and cross-linking. The digestion of protein in vivo depends on the accessibility and flexibility of the polypeptide chain. The structure of many proteins is destabilized by the acid conditions of the stomach that aids their hydrolysis and further destabilization by pepsin.