High-level production of creatine amidinohydrolase from Arthrobacter nicotianae 23710 in Escherichia coli.

In the present study, the gene encoding creatinase was amplified from Arthrobacter nicotianae 23710 (CICC) and functionally overexpressed in Escherichia coli. By applying a two-stage temperature control strategy, the production of creatinase was increased up to 61.3 U/mL in 3-L fermentor with a high productivity of 6.1 U/mL/h. The recombinant creatinase shows excellent resistance to the chelating agent EDTA, the surfactants (Tween 20, Tween 80, and Triton X-100) and the common preservative NaN3 (20 mM). High-level expression of the recombinant creatinase will contribute to its application in clinical diagnosis of renal function.