Pancreatin preferentially cleaves N-terminal phosphorylated regions, the C-terminal hydrophobic regions and the middle region of b-casein, the terminal regions of
as1-casein, and both the terminals and the middle region of
as2-casein [24] (Figure 1). Because of their specificities,the interactions between the peptides generated from enzymatic hydrolysis with pancreatin and/or trypsin may increase, resulting in hydrolysates with lesser protein
solubility compared to hydrolysates obtained using papain [17,24,25].