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The catalase genekatA ofLactobacillus sakei LTH677 was cloned and expressed inEscherichia coli UM2,Lactobacillus casei LK1, andLactobacillus curvatus LTH1432. The last host is a catalase-deficient plasmid-cured derivative of a starter organism used in meat fermentation. The regulation ofkatA expression was found to be the same inL. sakei LTH677 and the recombinant strains. The addition of H2 O2 to anaerobic cultures, as well as a switch to aerobic conditions, resulted in a strong increase in KatA activity. The expression was investigated in more detail withL. sakei LTH677 andL. curvatus LTH4002. The recombinant strain LTH4002 did not accumulate H2 O2 under glucose-limited aerobic conditions and remained viable in the stationary phase. Under inductive conditions, thekatA -specific mRNA and the apoenzyme were synthesized de novo. Deletion derivatives of thekatA promoter were produced, and the regulatory response was investigated by fusion to the β-glucuronidase reporter genegusA and expression inL. sakei LTH677. The fact that gene expression was subject to induction was confirmed at the level of transcription and protein synthesis. A small putative regulatory sequence of at least 25 bp was identified located upstream of the −35 site. Competition experiments performed withL. sakei LTH677 harboring the fusion constructs consisting of thekatA promoter andgusA revealed that an activator protein is involved in the transcriptional induction ofkatA.

Oxygen-Dependent Regulation of the Expression of the Catalase Gene katA of Lactobacillus sakei LTH677