Abstract
l-isoleucine dioxygenase (IDO) was considered as an important industrial biocatalyst for 4-hydroxyisoleucine synthesis. TIDO encoding gene tido from Bacillus thuringiensis TUST-1 was cloned and expressed to detect enzymatic characteristics of recombined IDO. Sequence analysis indicated that tido was composed of 723 nucleotides encoding 240 amino acids. K m and the V max of the recombinant IDO was 0.168 mmol/L and 2.283 μmol/min/mg, respectively. Enzymatic assays sh owed that the optimum temperature and pH for the recombinant IDO was 30 °C and 8.0 respectively, furthermore, the relative activity of the enzyme remained 82.2% after 6 h’ incubation at 30 °C. This work will lay practical basis on recombinant IDO production and microbial manufacture technology of 4-hydroxyisoleucine and other amino acid derivatives.
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Acknowledgements
This work was supported by National High Technology Research and Development Program 2013AA102106), by the National Natural Science Foundation of China (31300069); Tianjin Municipal Science and Technology Commission (grant No. 15JCTPJC62800); Tianjin Undergraduate Training Program for Innovation and Entrepreneurship (201510057063). China Postdoctoral Science Foundation Funded Project (2017M61170) and Innovation training program for college students in Tianjin(201710057039) need to be added as the last two supported project.
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Xue, N. et al. (2018). Characterization of Recombinant Dioxygenase from Bacillus thuringiensis . In: Liu, H., Song, C., Ram, A. (eds) Advances in Applied Biotechnology. ICAB 2016. Lecture Notes in Electrical Engineering, vol 444. Springer, Singapore. https://doi.org/10.1007/978-981-10-4801-2_18
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DOI: https://doi.org/10.1007/978-981-10-4801-2_18
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