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Table 1 Proteases commonly used for protein hydrolysis

From: Protein hydrolysates in animal nutrition: Industrial production, bioactive peptides, and functional significance

Class of enzyme Name of enzyme EC number Specific cleavage
Endopeptidases
 Aspartate protease Chymosin (rennin; pH 1.8–2) 3.4.23.4 the Phe-Met bond, clotting of milk
Pepsin A (pH 1.8–2) 3.4.23.1 Aromatic AAs, hydrophobic AAs
 Cysteine protease Bromelain (from pieapples) 3.4.22.4 Ala, Gly, Lys, Phe, Tyr
Cathepsin B 3.4.22.1 Arg, Lys, Phe
Ficain (ficin; from fig tree) 3.4.22.3 Ala, Asn, Gly, Leu, Lys, Tyr, Val
Papain (from papaya) 3.4.22.2 Arg, Lys, Phe
 Metallo protease Bacillolysin (Bacillus bacteria) 3.4.24.28 Aromatic AAs, Ile, Leu, Val
Thermolysin (Bacillus bacteria) 3.4.24.27 Aromatic AAs, Ile, Leu, Val
 Serine protease Chymotrypsin (pH 8–9) 3.4.21.1 Aromatic AAs, Leu
Subtilisin (from Bacillus bacteria) 3.4.21.14 Mainly hydrophobic AAs
Trypsin (pH 8–9) 3.4.21.4 Arg, Lys
Exopeptidases
 Aminopeptidases Aminopeptidasea 3.4.11.1 AA at the N-terminus of protein/peptide
Aminopeptidase Yb 3.4.11.15 Lys at the N-terminus of protein/peptide
 Carboxypeptidase Carboxypeptidasec 3.4.16.1 Acidic, neutral, and basic AAs
Glycine carboxypeptidased 3.4.17.4 Gly at the C-terminus of protein/peptide
Alanine carboxypeptidasee 3.4.17.8 D-Ala at the C-terminus of peptide
Carboxypeptidase Sf 3.4.17.9 Gly at the C-terminus of protein/peptide
 Dipeptidase Dipeptidase 1f 3.4.13.11 A wide range of dipeptides
Proline dipeptidase (prolidase)a 3.4.13.9 AA-Pro or -hydroxyproline at the C-terminus (not Pro-Pro)
Prolyl dipeptidasea 3.3.13.8 Pro-AA or Hydroxyproline-AA
Endo- and exo-peptidases
 Pronase A mixture of proteasesa (from Streptomyces griseus) 3.4.24 Acidic, neutral, and basic AAs
 Other peptidases Dipeptidyl-peptide IIIf 3.4.14.4 Release of an N-terminal dipeptide from a peptide comprising four or more AA residues, with broad specificity
Dipeptidyl-peptidase IVg 3.4.14.5 Release of an N-terminal dipeptide from a peptide consisting of prolineh
  1. Adapted from Kunst [16] and Dixon and Webb [17]. AA amino acid
  2. aMetallopeptidase (requiring Mn2+, Mg2+ or Zn2+ for activation)
  3. bMetallopeptidase (requiring Co2+ for activation; inhibited by Zn2+ and Mn2+)
  4. cSerine carboxypeptidase
  5. dStrongly inhibited by Ag+ and Cu2+
  6. eMetallopeptidase (requiring Mn2+, Mg2+, Zn2+, Ca2+ or Co2+ for activation)
  7. fMetallopeptidase (requiring Zn2+ for activation)
  8. gSerie protease
  9. hAA1-Pro-AA2, where AA2 is neither proline nor hydroxyproline