Carlsberg (EC 3.4.21.62). Subtilisin proteases are serine
proteases with relatively low substrate specificity, but
they preferentially cleave peptide bonds after large
non-b-branched hydrophobic residues [15]. Although
both enzymes had subtilisin activities, Alcalase1 2.4L
presents a specific activity of glutamyl endopeptidase that
is not present in Prolyve 100TM and is responsible for
cleaving peptide bonds after a glutamic acid and to a
lesser extent, aspartic acid residues. This explains its
ability to digest substrates with glutamic acid residues
at the C-terminus, such as casein phosphopeptides and
whey proteins [15,26]. The whey protein hydrolysates