Literature summary for 4.3.1.24 extracted from

Zhang, B.Z.; Cui, J.D.; Zhao, G.X.; Jia, S.R.
Modeling and optimization of phenylalanine ammonia lyase stabilization in recombinant Escherichia coli for the continuous synthesis of L-phenylalanine on the statistical-based experimental designs (2010), J. Agric. Food Chem., 58, 2795-2800.

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Application

Application	Comment	Organism
synthesis	improvement of recombinant phenylalanine ammonia-lyase stability in Escherichia coli during the enzymatic methods of L-phenylalanine production. The optimum values for testing variables are 13.04 mM glycerol, 1.87 mM sucrose, 4.09 mM DTT, and 69 mM Mg2+. The maximum phenylalanine ammonia-lyase activity is retained as 67.73 units/g after three successive cycles of bioconversion. In comparison to initial phenylalanine ammonia-lyase activity, the loss of phenylalanine ammonia-lyase activity was only 22%. Phenylalanine ammonia-lyase activity is enhanced about 23% in comparison to the control	Rhodotorula toruloides

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rhodotorula toruloides

Organism

Organism	UniProt	Comment	Textmining
Rhodotorula toruloides	-	-	-

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Release 2023.1 (January 2023)