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Literature summary for 3.4.17.1 extracted from

  • Vertesi, A.; Simon, L.M.; Kiss, I.; Szajani, B.
    Preparation, characterization and application of immobilized carboxypeptidase A (1999), Enzyme Microb. Technol., 25, 73-79.
No PubMed abstract available

Application

Application Comment Organism
synthesis immobilization for synthetic use Bos taurus
synthesis useful tools for peptide biosynthesis in non-conventional media, considered Bos taurus

General Stability

General Stability Organism
hydrophobic environment of immobilized enzyme enhances conformational stability Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.07
-
hippuryl-L-Phe soluble enzyme Bos taurus
1.65
-
hippuryl-L-Phe immobilized enzyme Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
comparison of activities of enzyme immobilized on different supports, highest activity for polyacrylamide bead support Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hippuryl-L-Phe + H2O
-
Bos taurus hippuric acid + L-Phe
-
ir

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 35 soluble enzyme Bos taurus
50 55 immobilized enzyme Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
35% activity after 30 min of immobilized enzyme, no activity of soluble enzyme Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Bos taurus
7.5 8 identical for soluble and immobilized enzymes Bos taurus

pH Stability

pH Stability pH Stability Maximum Comment Organism
8.5
-
quick inactivation of soluble enzyme, no inactivation of immobilized enzyme Bos taurus