“…While the proteases used in this study have specificity for the breakdown of proteins, Alcalase has a preference for large residue carboxyl sites without load of proteins and peptides links to adjacent hydrophobic or aromatic amino acids, such as tyrosine (Butré, Wierenga, & Gruppen, ; Paraman, Hettiarachchy, Schaefer, & Beck, ; Rossini, Noreña, Cladera‐Olivera, & Brandelli, ). Even though the specificities of Neutrase and Protamex are not clearly defined (Dryáková, Pihlanto, Marnila, Čurda, & Korhonen, ), it is known that they are endoproteases characterized by their ability to hydrolyze internal peptides bonds (Liu et al, ), which preferentially release hydrophobic amino acids: phenylalanine, isoleucine, leucine, methionine, and valine (Dijk, Folkertsma, & Dekker, ).…”