Literature summary for 3.5.1.11 extracted from

Montes, T.; Grazu, V.; Lopez-Gallego, F.; Hermoso, J.A.; Garcia, J.L.; Manso, I.; Galan, B.; Gonzalez, R.; Fernandez-Lafuente, R.; Guisan, J.M.
Genetic modification of the penicillin G acylase surface to improve its reversible immobilization on ionic exchangers (2007), Appl. Environ. Microbiol., 73, 312-319.

Protein Variants

Protein Variants	Comment	Organism
additional information	the mutant enzyme contains 85 exposed Glu-plus-Asp residues, while the native enzyme exposed in the surface only 77 acidic residues. Such an increase in the number of negative charges reduces the isoelectric point of the mutant enzyme from 6.4 to 4.3. 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, suggesting that these conditions allow the penetration of the enzyme inside the polymeric beds, thus becoming fully covered with the polymer. After the enzyme inactivation, it can be desorbed to reuse the support	Escherichia coli

General Stability

General Stability	Organism
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	Escherichia coli
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	Escherichia coli

Organism

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

Escherichia coli

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

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
penicillin G acylase	-	Escherichia coli

pI Value

Organism	Comment	pI Value Maximum	pI Value
Escherichia coli	wild-type enzyme	-	4.3
Escherichia coli	mutant enzyme	-	6.4