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- W3208134192 abstract "Enzymes possess a highly specific affinity toward their substrates. In this study, an enzyme-based biological method was established for chiral discrimination of D/L-tryptophan (Trp). The polydopamine modified magnetic particles (PDA@Fe3O4) were prepared for immobilization of the genetically engineered bacterium Escherichia coli (E. coli) DH5α. The bacteria-magnetic particles conjugates (bacteria@PDA@Fe3O4) demonstrate excellent chiral discrimination performance toward D/L-Trp at pH 7.0 and 45 °C. The investigation for the principle exhibits that the immobilized E. coli DH5α can produce tryptophanase, and the enzyme can selectively recognize and degrade L-Trp. The Michaelis constant of tryptophanase produced by bacteria@PDA@Fe3O4 was measured to be 25.7 µg mL-1. This method avoids the purification of tryptophanase and unlocks the potential of bacteria modified magnetic particles for chiral discrimination of racemic tryptophan." @default.
- W3208134192 created "2021-11-08" @default.
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- W3208134192 date "2021-12-01" @default.
- W3208134192 modified "2023-09-27" @default.
- W3208134192 title "Unlocking the potential of Escherichia coli modified magnetic particles for chiral discrimination of racemic tryptophan" @default.
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- W3208134192 doi "https://doi.org/10.1016/j.chroma.2021.462638" @default.
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