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3.5.1.11: penicillin amidase

This is an abbreviated version!
For detailed information about penicillin amidase, go to the full flat file.

Word Map on EC 3.5.1.11

Reaction

penicillin
+
H2O
=
a carboxylate
 +
6-aminopenicillanate

Synonyms

ACPGA001 PGA, AfPGA, alpha-acylamino-beta-lactam acylhydrolase, amidase, amidohydrolase, ampicillin acylase, AuAAC, benzylpenicillin acylase, BmPGA, Eca3205, KcPGA, maPGA, More, novozym 217, PA, PAC, penicillin acylase, penicillin amidase, Penicillin amidohydrolase, penicillin G acylase, Penicillin G amidase, Penicillin G amidohydrolase, penicillin V acylase, Penicillin V amidase, penicillin-G acylase, PGA, PGA650, PVA, semacylase, Sm-PVA, YxeI

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.11 penicillin amidase

General Stability

General Stability on EC 3.5.1.11 - penicillin amidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
amoxicillin synthesis activity of cross-linked enzyme aggregates and poly-lysine supported cross-linked enzyme aggregates is retained over twenty cycles. The amoxicillin synthesis activity of cross-linked enzyme aggregates gradually decreases. After twenty cycles, 73% of initial activity is retained. Poly-lysine supported cross-linked enzyme aggregates achieve excellent operational stability spanning twenty cycles. Poly-lysine supported cross-linked enzyme aggregates retain 97% of their initial activity after twenty conversion cycles
crosslinking with glutaraldehyde fails to protect the immobilized enzyme activity in case of proline, tryptophan, and casein acid hydrolysate
-
enzyme immobilized on alginate/chitosan hybrid beads can be reused more times as compared to enzyme immobilized on alginate beads
-
enzyme immobilized on alginate/chitosan hybrid beads shows higher operational stability compared to enzyme immobilized on alginate beads
-
immobilized enzyme, higher stability than soluble enzyme
-
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
the enzyme is more stable in [bmim]PF6 than in conventional aqueous solution
-
the mutant enzyme adsorbed on DEAE is more stable than the enzyme covalently immobilized on CNBr agarose. The most stable preparations are those where the enzyme is adsorbed on polyethyleneimine
-
the native enzyme does not become significantly immobilized on any of the three supports (DEAE and two supports coated with polyethyleneimine of different sizes), while the mutant enzyme becomes fully immobilized on them. The use of restrictive conditions during the enzyme adsorption on anionic exchangers (pH 5 and high ionic strength) further increases the strength of adsorption and the enzyme stability in the presence of organic solvents
-