Objective Identification and characterization of a novel thermostable amidase (Xam) with wide pH tolerance and broad-spectrum substrate specificity. Results Xam was identified from non-thermophilic Xinfangfangia sp. DLY26 and its acyl transfer activity was investigated. Recombinant Xam was optimally active at 60 degrees C and pH 9.0. The enzyme had a half life of 18 h at 55 degrees C and maintained more than 60 % of its maximum activity in the range of pH 3.0-11.0. Additionally, Xam exhibited broad substrate specificity towards aliphatic, aromatic, and heterocyclic amides. Conclusions These unique properties make Xam a promising biocatalyst for production of important hydroxamic acids at elevated temperatures.

Thermostable amidase; Xinfangfangia sp. DLY26; Cloning; Characterization

China University of Petroleum (Huadong)