Programming a bacterial biosensor for directed evolution of tryptophan hydroxylase via high-throughput droplet sorting

Biosens Bioelectron. 2025 Mar 1:271:117072. doi: 10.1016/j.bios.2024.117072. Epub 2024 Dec 17.

Abstract

The modification of tryptophan hydroxylase (TPH) for the biosynthesis of 5-hydroxytryptophan (5-HTP) has recently become a focus of research. In this study, we established a droplet-based ultrahigh-throughput microfluidic screening platform (DTSP) to improve the industrial properties of TPH, whereas a bacterial biosensor for L-tryptophan (L-Trp) detection was engineered to improve sensitivity. The promoter pJ23111 achieved a strong negative correlation between the L-Trp concentration and the fluorescence output of the biosensor. The optimized DTSP platform was then utilized to screen superior TPH mutants by employing iterative saturation mutagenesis (ISM). The M4-1 variant (D129L/Q132M/P103A/T236K) demonstrated a 4.25-fold increase of catalytic activity compared to the parental CviPAH. Moreover, it exhibited excellent thermostability, with a 3.2-fold increase of half-life at 45 °C. Our study provides a reference for the development of bacterial biosensors for microdroplet-based screening platforms.

Keywords: 5-Hydroxytryptophan; Biosensor; Droplet-based microfluidic screening; Molecular dynamics simulations; Tryptophan hydroxylase.

MeSH terms

  • 5-Hydroxytryptophan / chemistry
  • Biosensing Techniques* / methods
  • Directed Molecular Evolution*
  • Escherichia coli / genetics
  • Escherichia coli / isolation & purification
  • High-Throughput Screening Assays / methods
  • Tryptophan Hydroxylase* / genetics
  • Tryptophan Hydroxylase* / metabolism
  • Tryptophan* / chemistry
  • Tryptophan* / metabolism

Substances

  • Tryptophan Hydroxylase
  • Tryptophan
  • 5-Hydroxytryptophan