Thermostable tryptophan synthase of Bacillus stearothermophilus expressed in Escherichia coli
1990
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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