Purification and Characterization of Nit _phym , a Robust Thermostable Nitrilase From Paraburkholderia phymatum.

ABSTRACT: Despite the success of some nitrilases in industrial applications, there is a constant demand to broaden the catalog of these hydrolases, especially robust ones with high operational stability. By using the criteria of thermoresistance to screen a collection of candidate enzymes heterologously expressed in Escherichia coli, the enzyme Nit _phym from the mesophilic organism Paraburkholderia phymatum was selected and further characterized. Its quick and efficient purification by heat treatment is of major interest for large-scale applications. The purified nitrilase displayed a high thermostability with 90% of remaining activity after 2 days at 30°C and a half-life of 18 h at 60°C, together with a broad pH range of 5.5-8.5. Its high resistance to variou

SUBMITTER: Bessonnet T 

PROVIDER: S-EPMC8280356 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature