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Suitability of different β-galactosidases as reporter enzymes in Bacillus subtilis

Appl Microbiol Biotechnol. 2012 Jan;93(1):381-92. doi: 10.1007/s00253-011-3645-0. Epub 2011 Nov 4.

Abstract

The suitability of three β-galactosidases as reporter enzymes for promoter expression analyses was investigated in Bacillus subtilis with respect to various temperature conditions during cultivation and assay procedures. Starting from the hypothesis that proteins derived from diverse habitats have different advantages as reporters at different growth temperatures, the beta-galactosidases from the thermophilic organism Bacillus stearothermophilus, from the mesophilic bacterium Escherichia coli and from the psychrophilic organism Pseudoalteromonas haloplanktis TAE79 were analysed under control of the constitutive B. subtilis lepA promoter. Subsequent expression of the β-galactosidase genes and determination of specific activities was performed at different cultivation and assay temperatures using B. subtilis as host. Surprisingly, the obtained results demonstrated that the highest activities over a broad cultivation temperature range were obtained using the β-galactosidase from the mesophilic bacterium E. coli whereas the enzymes from the thermophilic and psychrophilic bacteria revealed a more restricted usability in terms of cultivation temperature.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Artificial Gene Fusion
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics*
  • Bacillus subtilis / growth & development
  • Cloning, Molecular
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Gene Expression
  • Gene Expression Profiling / methods*
  • Genes, Reporter*
  • Geobacillus stearothermophilus / enzymology
  • Geobacillus stearothermophilus / genetics
  • Promoter Regions, Genetic
  • Pseudoalteromonas / enzymology
  • Pseudoalteromonas / genetics
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Temperature
  • beta-Galactosidase / genetics*
  • beta-Galactosidase / metabolism*

Substances

  • Recombinant Proteins
  • beta-Galactosidase