Genetically engineered bacterium-modified magnetic particles assisted chiral recognition and colorimetric determination of D/L-tryptophan in millets.

Chiral recognition of enantiomers has always been a thorny issue since they exhibit the same properties under an achiral environment. Herein, polydopamine-functionalized magnetic particles (MP@PDA) were synthesized to immobilize the genetically engineered bacterium Escherichia coli DH5α (MP@PDA-E. coli). L-tryptophan (Trp) instead of D-Trp can be stereo-specifically degraded by tryptophanase in E. coli. The degradation product indole reacts with 4-dimethylaminobenzaldehyde to generate a rose-red adduct. Thus, MP@PDA-E. coli was employed to fabricate a chiral colorimetric method for chiral recognition and determination of L-Trp. The method averts the purification of tryptophanase. More importantly, tryptophanase demonstrates excellent enantioselective ability for L-Trp. The method can not only quantitatively detect L-Trp but also realize the measurement of the enantiomer percentage in the enantiomeric mixture. The feasibility was verified by detecting L-Trp in millet samples from different origins. Furthermore, a portable device was fabricated to make the method more convenient.