Enzymatic debittering of food protein hydrolysates

Peptides: Production, bioactivity, functionality, and applications

“…Hydrophobic amino acids caused more bitterness when they were inside the peptide chain rather than the N-or C-terminus of peptides (Matoba and Hata, 1972). FitzGerald and O'Cuinn (2006) listed different methods of removing bitterness from protein hydrolysates: (i) absorption of bitter peptides on activated carbon; (ii) chromatographic removal using different matrices; (iii) selective extraction with alcohols; (iv) masking hydrolysates by addition of polyphosphates, specific amino acids such as Asp and Glu, and a-cyclodextrins; (v) mixing hydrolysates with intact protein samples; (vi) formation of plasteins; and (vii) cross-linking using transglutaminase. However, they also pointed to drawbacks of these methods such as loss of some amino acid residues and decrease in solubility.…”

Antihypertensive Peptides from Food Proteins

“…Peptidase-mediated debittering has also been applied. This involves the concomitant or sequential incubation of the protein hydrolysates with exopeptidases, with priority cleavage at hydrophobic residues [126]. However, these debittering strategies may lead to the loss of some amino acid residues from hydrolysates.…”

Solvent and thermal stability, and pH kinetics, of proline-specific dipeptidyl peptidase IV-like enzyme from bovine serum

“…Aside from any intracellular role, aminopeptidases have applications in debittering casein hydrolysates [12,13]. In the food industry, Pro-containing peptides are associated with bitter flavours, yet few Pro-cleaving enzymes have been exploited to date in debittering [12][13][14][15].…”

“…In the food industry, Pro-containing peptides are associated with bitter flavours, yet few Pro-cleaving enzymes have been exploited to date in debittering [12][13][14][15]. The proline specificity of DPP IV suggests that it may have potential as a biocatalyst for peptide processing in-vitro.…”