Table 2. Enzymes which can potentially be used for degradation of oilseed cell membranes and oleosome membranes.
| Enzyme | Origin/Producer | Substrate | Reaction product | Ref. |
|---|---|---|---|---|
| Proteases | ||||
| Serine proteases (Exopeptidases) | ||||
| Carboxypeptidase Y EC 3.4.16.5 |
Saccharomyces cerevisiae | Proteins with C-terminal side of the amino acids with broad specificity | Peptide and proteinogenic amino acid | (60) |
| Metalloproteases (Exopeptidases) | ||||
| Carboxypeptidase A EC 3.4.17.1 |
Bovine pancreas | Proteins with C-terminal side of the amino acids, but has little or no action Asp, Glu, Arg, Lys or Pro | Peptide and l-amino acid | (60) |
| Carboxypeptidase B EC 3.4.17.2 |
Porcine pancreas | Hydrolysis of proteins with C-terminal side of the Lys or Arg amino acids | Peptide and l-amino acid (l-Lys or l-Arg) | (60, 61) |
| Serine proteases (Endopeptidases) | ||||
| Trypsin EC 3.4.21.4 |
Porcine pancreas | Protein at positions Arg-|-, Lys-|- | Peptide | (60-63) |
| Elastase EC 3.4.21.36 |
Porcine pancreas | Proteins, including elastin, at position Ala-|- | Peptide | (60, 61) |
| Proteinase K EC 3.4.21.64 |
Tritirachium album | Peptide amides and proteins, including keratin | Peptide | (60, 64) |
| Cysteine proteases (Endopeptidases) | ||||
| Papain EC 3.4.22.2 |
Latex of the papaya (Carica papaya) fruit | Proteins with broad specificity, especially an amino acid bearing a large hydrophobic side chain at the P2 position, and protein at positions Arg-|-, Lys-|- | Peptide | (58,60, 65,66) |
| Stem bromelain EC 3.4.22.32 |
Stem of pineapples (Ananas comosus) | Proteins with broad specificity, but strong preference for Z-Arg-Arg-|-NHMec amongst small molecule substrates | Peptide | (58,60, 67,68) |
| Fruit bromelain EC 3.4.22.33 |
Fruit of pineapples (Ananas comosus) | Proteins with broad specificity, especially the Bz-Phe-Val-Arg-|-NHMec links, but no action on Z-Arg-Arg-NHMec | Peptide | (58,60, 67,68) |
| Ficin (ficain) EC 3.4.22.3 |
Latex of the fig (Ficus carica, Ficus glabrata) | Proteins with broad specificity, similar to that of papain | Peptide | (60, 69) |
| Aspartic proteases (Endopeptidases) | ||||
| Pepsin (pepsin A) EC 3.4.23.1 |
Porcine gastric mucosa | Protein Phe (or Tyr, Leu, Trp)-|- Trp (or Phe, Tyr, Leu) links | Peptide | (60, 70) |
| Aspergillopepsin I EC 3.4.23.18 |
Aspergillus species | Proteins with broad specificity | Peptide | (71) |
| Penicillopepsin EC 3.4.23.20 |
Penicillium janthinellum | Proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues | Peptide | (71) |
| Rhizopuspepsin EC 3.4.23.21 |
Rhizopus chinensis,
R. niveus |
Proteins with broad specificity, prefers hydrophobic residues, clots milk, and activates trypsinogen | Peptide | (71) |
| Saccharopepsin EC 3.4.23.25 |
Saccharomyces cerevisiae | Proteins with broad specificity for peptide bonds | Peptide | (71) |
| Metalloproteases (Endopeptidases) | ||||
| Thermolysin EC 3.4.24.27 |
Bacillus thermoproteolyticus | Protein Leu (or Phe)-|- Leu (or Phe, Val, Met, Ala, Ile) links | Peptide | (60, 72, 73) |
| Phospholipases | ||||
| Phospholipase A1 EC 3.1.1.32 |
Aspergillus oryzae | Broad specificity, but prefers phosphatidyl choline | Lysophosphatidyl choline and fatty acid | (74, 75) |
| Phospholipase A2 EC 3.1.1.4 |
Honey bee venom (Apis mellifera), bovine pancreas | Ester linkage at sn-2 carbon of fatty acid acyl bond of phospholipids, preferring phospholipids containing arachidonic acid | Lysophospholipid and free fatty acid | (74, 76-79) |
| Phospholipase C EC 3.1.4.3 |
Bacillus cereus, Clostridium perfringens | The bond between the acylglycerol and the phosphate group, prefers phosphatidyl choline, phosphatidyl ethanolamine, sphingomyelin and phosphatidyl inositol | 1,2-Diacyl-sn-glycerol and phosphate monoester | (74, 75, 80-83) |
| Phospholipase D EC 3.1.4.4 |
Streptomyces sp., peanut (Arachis hypogaea) | Phosphate diester bond of glycerophosphatides containing choline, ethanolamine, serine, or glycerol, preferring phosphatidyl choline | Phosphatidic acid and choline | (74, 84, 85) |
| Phosphatases | ||||
| Alkaline phosphatase EC 3.1.3.1 |
Escherichia coli, bovine intestinal mucosa | Phosphate monoester | Alcohol and phosphate | (59, 86-88) |
| Protein phosphatase EC 3.1.3.16 |
Escherichia coli, bovine kidneys, bovine brain | Serine- or threonine-bound phosphate group from a wide range of phosphoproteins | Protein (containing Ser/Thr) and phosphate | (59, 89-91) |
| Acid phosphatase EC 3.1.3.2 |
Lupin seeds (Lupinus luteus), potato tubers | Phosphate monoester | Alcohol and phosphate | (59, 92) |
| Phosphatidate phosphatase EC 3.1.3.4 |
Cotton seed (Gossypium hirsutum L.), Saccharomyces cerevisiae | 1,2-Diacyl-sn-glycerol-3-phosphate | 1,2-Diacyl-sn-glycerol and phosphate | (59, 93-96) |