Summary
The tryptophan synthase genes,trpA andtrpB, from a moderate thermophile,Bacillus stearothermophilus IFO13737, were expressed efficiently inEscherichia coli. The recombinant tryptophan synthase amounted to 22% of the soluble cellular protein, and was purified to homogeneity by three steps. The enzyme is more thermostable thanE.coli tryptophan synthase, especially the α subunit. The enzyme is also more resistant to sodium dodecylsulfate and methanol thanE.coli enzyme.
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Ishiwata, Ki., Suzuki, T., Iwamori, S. et al. Thermostable tryptophan synthase ofBacillus stearothermophilus expressed inEscherichia coli . Biotechnol Lett 12, 185–190 (1990). https://doi.org/10.1007/BF01026796
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DOI: https://doi.org/10.1007/BF01026796