Enterokinase is a serine protease that recognizes the amino acid sequence with a high specificity. The enterokinase activates its natural substrate trypsinogen and releases trypsin by cleavage at the C-terminal end of this sequence. The aspartic acid residues can be partially substituted by glutamic acid.
Enterokinase cleavage is carried out at an enzyme/substrate ratio (w/w) of 1/20-1/200 for 1-24 h. For each fusion protein pilot experiments should be done to find out suitable conditions.
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