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Updated: Jan 23, 2026

Pyrosequencing for Microbial Identification and Characterization
Published on: August 22, 2013
Identification and characterization of an amidase from Leclercia adecarboxylata for efficient biosynthesis of
Xue-Mei Kang1, Xue Cai1, Zhi-Qiang Liu1
1The National and Local Joint Engineering Research Center for Biomanufacturing of Chiral Chemicals, Zhejiang University of Technology, Hangzhou 310014, People's Republic of China; Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310014, People's Republic of China.
Abstract:
L-phosphinothricin (L-PPT) is an important broad-spectrum herbicide with expanding utilization because it is environmentally benign. A strain Leclercia adecarboxylata ZJB-17008 with capability of catalyzing rac-4-(hydroxy(methyl)phosphoryl)-2-(2-phenylacetamido) butanoic acid (rac-S) to L-PPT was screened and identified, from which an amidase (La-Ami) was cloned and secretory expressed in Bacillus subtilis WB 800 for the bioproduction of L-PPT. The recombinant La-Ami exhibited an excellent enantioselectivity (99.9% ee) and remarkable thermostability with a half-life of 19.8 h at 50 °C. Furthermore, La-Ami displaying a high space-time yield of 787.2 g L-1 d-1 at 50 °C and pH 8.5 under the rac-S concentration of 500 mM (150 g L-1). The finally refined L-PPT was obtained with a purity of 99% and a total yield reached 90%. These results implying that this secretory expressed amidase La-Ami is possible to be applied in the large-scale bioproduction of L-PPT.
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