Covalent immobilization of recombinant Citrobacter koseri transaminase onto epoxy resins for consecutive asymmetric synthesis of L-phosphinothricin

Transaminase responsible for alienating prochiral ketone compound is applicable to asymmetric synthesis of herbicide L-phosphinothricin (L-PPT). In this work, the covalent immobilization of recombinant transaminase from Citrobacter koseri (CkTA) was investigated on different epoxy resins. Using opti...

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Published in:Bioprocess and biosystems engineering 2020-09, Vol.43 (9), p.1599-1607
Main Authors: Jia, Dong-Xu, Xu, Hai-Peng, Sun, Chen-Yi, Peng, Chen, Li, Jun-Liang, Jin, Li-Qun, Cheng, Feng, Liu, Zhi-Qiang, Xue, Ya-Ping, Zheng, Yu-Guo
Format: Article
Language:English
Subjects:
Amino acids
Asymmetric synthesis
Asymmetry
Biocatalysts
Biotechnology
Chemistry
Chemistry and Materials Science
Citrobacter
Citrobacter koseri
Environmental Engineering/Biotechnology
Enzymes
Epoxy resins
Food Science
Herbicides
Immobilization
Industrial and Production Engineering
Industrial Chemistry/Chemical Engineering
Optimization
Phosphinothricin
Polymers
Research Paper
Substrates
Synthesis
Thermal stability
Transaminase
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Summary:Transaminase responsible for alienating prochiral ketone compound is applicable to asymmetric synthesis of herbicide L-phosphinothricin (L-PPT). In this work, the covalent immobilization of recombinant transaminase from Citrobacter koseri (CkTA) was investigated on different epoxy resins. Using optimum ES-105 support, a higher immobilized activity was obtained via optimizing immobilization process in terms of enzyme loading, coupling time and initial PLP concentration. Crucially, due to blocking unreacted epoxy groups on support surface with amino acids, the reaction temperature of blocked immobilized biocatalyst was enhanced from 37 to 57 °C. Its thermostability at 57 °C was also found to be superior to that of free CkTA. The K m value was shifted from 36.75 mM of free CkTA to 39.87 mM of blocked immobilized biocatalyst, demonstrating that the affinity of enzyme to the substrate has not been apparently altered. Accordingly, the biocatalyst performed the consecutive synthesis of L-PPT for 11 cycles (yields>91%) with retaining more than 91.13% of the initial activity. The seemingly the highest reusability demonstrates this biocatalyst has prospective for reducing the costs of consecutive synthesis of L-PPT with high conversion.
ISSN:1615-7591
1615-7605
DOI:10.1007/s00449-020-02351-3