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Hydrolysis degree, peptide profile and phenylalanine removal from whey protein concentrate hydrolysates obtained by various proteases

2012; Wiley; Volume: 48; Issue: 3 Linguagem: Inglês

10.1111/ijfs.12003

1365-2621

M. P. C. Silvestre, Maitê C. da Silva, Mariana Wanessa Santana de Souza, Viviane Dias Medeiros Silva, Marcos José Burle de Aguiar, Mauro R. Silva,

Enzyme Production and Characterization

Summary The action of various proteases was tested for preparing whey protein concentrate ( WPC ) hydrolysates with high degree of hydrolysis ( DH ), appropriate peptide profiles and reduced phenylalanine ( P he) content. The peptide profile analysis included the fractionation of hydrolysates by size‐exclusion HPLC . The rapid correct fraction area method was used to quantify the components of the chromatographic fractions. Activated carbon ( AC ) was used to remove Phe, and its efficiency was evaluated by measuring the amount of Phe by second‐derivative spectrophotometry. The results showed that the DH of WPC hydrolysates increased and that the protease from A spergillus oryzae yielded the highest DH value. This protease also produced the best peptide profile, that is, the highest di‐ and tripeptide content (16.14%), the highest amounts of free amino acids (18.43%) and the lowest amount of large peptides (18.76%). The proteases from both A . oryzae and B acillus subtilis produced the highest Phe removals (79.0 and 77.8%, respectively).