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Characterization and improvement of substrate-binding affinity of D-aspartate oxidase of the thermophilic fungus Thermomyces dupontii.

Appl. Microbiol. Biotechnol.. 2019; 
TakahashiShouji,OsugiKohei,ShimekakeYuya,ShinboAkira,AbeKatsumasa,KeraYo
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Bacterial Expression System … The full length of the TdDAAO gene (Talth1p4_001973) without predicted introns was synthesized based on the codon usage of E. coli by GenScript (Piscataway, NJ, USA) and ligated into NdeI and BamHI sites of pET15b to obtain the expression vector pET15bTdDAAO in E … Get A Quote

摘要

D-Aspartate oxidase (DDO) is a valuable enzyme that can be utilized in the determination of acidic D-amino acids and the optical resolution of a racemic mixture of acidic amino acids, which require its higher stability, higher catalytic activity, and higher substrate-binding affinity. In the present study, we identified DDO gene (TdDDO) of a thermophilic fungus, Thermomyces dupontii, and characterized the recombinant enzyme expressed in Escherichia coli. In addition, we generated a variant that has a higher substrate-binding affinity. The recombinant TdDDO expressed in E. coli exhibited oxidase activity toward acidic D-amino acids and a neutral D-amino acid, D-Gln, with the highest activity to... More

关键词

D-Aspartate oxidase,E. coli expression,Site-directed mutagenesis,Thermomyces dupontii,Thermophilic fungus,Thermost