The differences in ACE inhibitory activities might be due to the
different hydrophilic–hydrophobic properties and to the different molecular
weights and amino acid sequences of ACE inhibitory peptides
present in protein hydrolysates. It has been shown that the highly hydrophilic propertymay have made the peptide inaccessible to the active
site of ACE, since the hydrophilic–hydrophobic balance is an important
factor in biologically activemolecules [66]. This can explain the low
activity of TRMH-Crude since it contains a high amount of hydrophilic
peptides.