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Optimizing Protein-Glutaminase Expression in Bacillus subtilis.

Xiaoying Ouyang1, Yingjie Liu1, Ruidan Qu1

  • 1School of Life Science, East China Normal University, 500 Dongchuan Road, Shanghai, 200241, People's Republic of China.

Current Microbiology
|March 19, 2021
PubMed
Summary
This summary is machine-generated.

This study optimized protein-glutaminase (PG) expression in Bacillus subtilis for industrial applications. Successful secretion and activation strategies were developed, paving the way for large-scale PG production in the food industry.

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Area of Science:

  • Biotechnology
  • Enzymology
  • Food Science

Background:

  • Protein-glutaminase (PG) is a valuable enzyme for modifying protein properties.
  • Industrial application of PG is hindered by low enzyme production from native sources like Chryseobacterium proteolyticum.

Purpose of the Study:

  • To investigate and optimize strategies for expressing PG in Bacillus subtilis.
  • To characterize the enzymatic properties of the expressed PG.

Main Methods:

  • Expression of PG from C. proteolyticum in B. subtilis WB800N, B. subtilis 168 (BS168), and DB403.
  • Analysis of PG secretion, activation (self-processing vs. exogenous proteases), and specific activity.
  • Determination of optimal pH, temperature, and cofactor effects (Mg2+, Ca2+, Zn2+) on PG activity.

Main Results:

  • PG was successfully secreted in B. subtilis WB800N, BS168, and DB403.
  • Active PG was secreted via self-processing in BS168 and DB403, while PG from WB800N required exogenous protease digestion.
  • Purified PG exhibited a specific activity of 20.9 U/mg, with optimal activity at pH 5.5 and 55°C, and stability across a pH range of 3.5-6.5. Divalent cations stabilized and activated the enzyme.

Conclusions:

  • Optimized expression strategies in B. subtilis enable efficient PG production.
  • Characterized enzymatic properties and stability support PG's potential in food industry applications.
  • This research provides a foundation for industrial-scale PG production.