Cloning and characterization of a novel thermostable amidase, Xam, from Xinfangfangia sp. DLY26

作者：Xi, Lijun; Tan, Wenfei; Li, Jing; Qu, Jianbo; Liu, Jianguo^*

来源：Biotechnology Letters, 2021, 43(7): 1395-1402.

DOI：10.1007/s10529-021-03124-y

• Thermostable amidase
• Xinfangfangia sp. DLY26
• Cloning
• Characterization

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.

• 出版日期2021-7
• 单位中国石油大学（华东）