Literature summary for 3.5.5.1 extracted from

Kumar, S.; Mohan, U.; Kamble, A.L.; Pawar, S.; Banerjee, U.C.
Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis (2010), Biores. Technol., 101, 6856-6858.

Search for more literature for 3.5.5.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Pseudomonas putida

General Stability

General Stability	Organism
nitrilase aggregates are prepared using ammonium sulfate (35%) precipitation followed by cross-linking with glutaraldehyde (125 mM) which renders 70% activity retention	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-
Pseudomonas putida MTCC 5110	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
35% (w/v) ammonium sulfate precipitation	Pseudomonas putida

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
mandelonitrile + 2 H2O	-	Pseudomonas putida	mandelic acid + NH3	-	?
mandelonitrile + 2 H2O	-	Pseudomonas putida MTCC 5110	mandelic acid + NH3	-	?

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
4	-	activity of cross-linked enzyme aggregate preparation remains stable up to 75 h at 4°C while the free enzyme loses 90% activity at this temperature in 75 h	Pseudomonas putida

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	the activity in the CLEA increases with the increase in the pH of cross-linking solution and it is maximum at pH 7.0	Pseudomonas putida

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Release 2023.1 (January 2023)