Introduction of two mutations into AroG increases phenylalanine production in Escherichia coli |
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Authors: | Rui Ding Lifei Liu Xuhui Chen Zhenhai Cui Ao Zhang Daming Ren Lijun Zhang |
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Affiliation: | 1. College of Agronomy, Shenyang Agricultural University, Shenyang, Liaoning, People’s Republic of China 3. College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang, Liaoning, People’s Republic of China 2. Liaoning Province Research Center of Plant Genetic Engineering Technology, Shenyang, Liaoning, People’s Republic of China
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Abstract: | l-Phenylalanine is an important amino acid commercially, and therefore optimization of its manufacture is of interest. We constructed a range of mutant alleles of AroG, the enzyme involved in the first step of phenylalanine biosynthesis. Three single-site mutant alleles were constructed (aroG8, aroG15, and aroG29), which were then combined to generate three double-site aroG fbr mutant alleles (aroG8/15, aroG8/29, and aroG15/29). Enzymatic activity, feedback inhibition, and fermentation were analyzed in all of the mutants. All double-site mutants, except AroG15/29, showed higher enzymatic activity and greater resistance to feedback inhibition than their respective single-site mutants. The E. coli strain carrying the aroG8/15 allele produced a phenylalanine titer of 26.78 g/l, a 116 % improvement over the control phenylalanine overproducing strain (12.41 g/l). Our findings provide an effective method for modifying phenylalanine biosynthetic genes, which may be applied to optimize the commercial manufacture of phenylalanine. |
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