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BRENDA support

Literature summary for 3.5.1.11 extracted from

  • Ayakar, S.; Yadav, G.
    Development of novel support for penicillin acylase and its application in 6-aminopenicillanic acid production (2019), Mol. Catal., 476, 110484 .
No PubMed abstract available
Search for more literature for 3.5.1.11

General Stability

General Stability Organism
the enzyme is covalently immobilized on aminopropyl functionalized mesocellular foam silica and is further cross-linked using glutaraldehyde without deactivation and upto 95% efficiency. The resulting biocatalyst has an activity of 1185 IU mg/l and demonstrates improved pH and thermal stability Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
penicillin G the enzyme is covalently immobilized on aminopropyl functionalized mesocellular foam silica and is further cross-linked using glutaraldehyde without deactivation and upto 95% efficiency. The resulting biocatalyst demonstrates improved resistance to the substrate and product inhibition Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P06875
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
penicillin G + H2O
-
 Escherichia coli phenylacetic acid + 6-aminopenicillanic acid
-
 ?

Synonyms

Synonyms Comment Organism
penicillin G acylase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 enzyme is covalently immobilized on aminopropyl functionalized mesocellular foam silica and is further cross-linked using glutaraldehyde Escherichia coli
50 60 soluble enzyme Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 60 30°C: about 65% of maximal activity, 50-60°C: maximal activity, soluble enzyme Escherichia coli
30 60 30°C: about 65% of maximal activity, 60°C: about 80% of maximal activity, enzyme is covalently immobilized on aminopropyl functionalized mesocellular foam silica and is further cross-linked using glutaraldehyde Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 enzyme is covalently immobilized on aminopropyl functionalized mesocellular foam silica and is further cross-linked using glutaraldehyde Escherichia coli
7.5
-
 soluble enzyme Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 pH 6.5: about 70% of maximal activity, pH 8.5: about 70% of maximal activity, enzyme is covalently immobilized on aminopropyl functionalized mesocellular foam silica and is further cross-linked using glutaraldehyde Escherichia coli
6.5 8.5 pH 6.5: about 85% of maximal activity, pH 8.5: about 90% of maximal activity Escherichia coli