Quantitative Analysis of Bacillus pumilus Serine Proteinases in Recombinant Bacillus Strains View Full Text


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Article Info

DATE

2022-03-28

AUTHORS

A. O. Koryagina, F. R. Osmanova, A. A. Toymentseva, A. V. Laikov, M. R. Sharipova

ABSTRACT

A comparative study of the expression of B. pumilus extracellular serine proteinases (subtilisin-like proteinase and glutamyl endopeptidase) under the control of different promoters and signal peptides based on the LIKE expression system in various B. subtilis recipient strains was carried out using mass spectral analysis in the monitoring of multiple reactions (MRM) mode. The maximum expression of the subtilisin-like proteinase was established under the control of a simulated signal peptide (SPAsp) and an inducible promoter of the PLiaI—LIKE expression system in the protease-deficient strain B. subtilis 20-36; the amount of secreted protein was 1.6 µg/µL of the culture liquid. The optimal expression of glutamyl endopeptidase was established under the control of the signal peptide of the Bacillus megaterium glycoside hydrolase gene (SPYngk) and the inducible promoter PLiaI in the protease-deficient strain B. subtilis 20-36, the maximum amount of protein was 0.06 µg/µL. It was concluded that selection of all components of the expression system for individual secreted proteins is of importance, including the selection of the optimal signal peptide. More... »

PAGES

199-206

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0026261722020060

DOI

http://dx.doi.org/10.1134/s0026261722020060

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1146629951


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