Unlocking the potential of Escherichia coli modified magnetic particles for chiral discrimination of racemic...

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.