A process for debittering casein and soy protein hydrolysates based on the application of hydrophobic chromatography to peptide solutions is described. During chromatography, binding forces occurring between the structurally similar phenolic resin and peptide amino acid residues containing aromatic/heterocyclic side chains delay the emergence of these bitter components and permits the selective preparation of a non‐bitter peptide hydrolysate. Characterization of the nonbitter and bitter peptide fractions, based on amino acid content is reported. Applications involving the use of the nonbitter peptide fractions as a protein supplement to foods and beverages are evaluated.
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Roland et al. (1978) studied this question.
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