Demonstrates efficient l-tryptophan production in Escherichia coli, suggesting new engineering strategies.
variants through two rounds of error-prone PCR and utilized a biosensor employing a green fluorescent protein to report l-serine consumption for screening TrpS mutants. Mutant C10 showed a 375% increase in enzyme activity compared with strain BS. Computational analysis was used to explore an improved catalytic mechanism. Finally, through systematic process optimization and catalytic strategy, strain C10 produced 94.2 g/L of l-tryptophan, the highest titer via whole-cell transformation. This study provides new perspectives and strategies for TrpS engineering and the industrial production of l-tryptophan.
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Chen et al. (2026) studied this question.
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