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Stabilizing displayed proteins on vegetative Bacillus subtilis cells.

Grace L Huang1,2, Jason E Gosschalk1, Ye Seong Kim1

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles, 611 Charles Young Drive East, Los Angeles, CA, 90095, USA.

Applied Microbiology and Biotechnology
|May 26, 2018
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Summary

Genetically modifying Bacillus subtilis to reduce proteases enhances displayed protein levels for biotechnology. Strain BRB08 shows superior stable protein display, with inhibitors further improving performance.

Keywords:
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Area of Science:

  • Microbial biotechnology
  • Protein engineering
  • Synthetic biology

Background:

  • Bacillus subtilis is a Gram-positive bacterium used industrially for enzyme production.
  • Engineered microbes displaying heterologous proteins have applications in biocatalysis, bioremediation, and biosensing.
  • Optimizing protein display on microbial surfaces is crucial for biotechnological advancements.

Purpose of the Study:

  • To investigate factors affecting displayed protein stability and copy number in Bacillus subtilis.
  • To compare the efficacy of different protease-deficient B. subtilis strains for displaying a Cel8A-LysM reporter protein.
  • To identify optimal conditions for stable, whole-cell protein display.

Main Methods:

  • Systematic comparison of four protease-deficient B. subtilis strains (WB800, BRB07, BRB08, BRB14).
  • Display of a Cel8A-LysM reporter protein (Clostridium thermocellum Cel8A fused to LysM modules).
  • Whole-cell cellulase measurements, fractionation experiments, and addition of chemical protease inhibitors.

Main Results:

  • Genetic elimination of extracytoplasmic proteases significantly improved Cel8A-LysM display levels.
  • Cellular autolysis in stationary phase led to a dramatic decrease in displayed protein for all strains.
  • Chemical protease inhibitors partially overcame autolysis, increasing protein display.
  • Strain BRB08 demonstrated the highest stable Cel8A-LysM accumulation without growth impairment or secretion stress.
  • A two-step procedure yielded enzyme-coated vegetative B. subtilis cells with stable activity for nearly 3 days.

Conclusions:

  • Reducing bacterial proteases is key to enhancing heterologous protein display on Bacillus subtilis.
  • Strain BRB08 is a suitable host for stable Cel8A-LysM display.
  • Protease inhibitors can mitigate protein loss due to autolysis.
  • Developed methods enable stable, whole-cell enzyme activity for biotechnological applications.