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Lactobacillus johnsonii La1, a probiotic bacterium with demonstrated health effects, grows in milk, where it ferments lactose tod - andl -lactate in a 60:40% ratio. Thed -lactate dehydrogenase (D-LDH) gene (ldhD ) of this strain was isolated, and an in vitro-truncated copy of that gene was used to inactivate the genomic copy in two strains, La1 and N312, by gene replacement. For that, an 8-bp deletion was generated within the clonedldhD gene to inactivate its function. The plasmid containing the alteredldhD was transferred toL. johnsonii via conjugative comobilization withLactococcus lactis carrying pAMβ1. Crossover integrations of the plasmid at the genomicldhD site were selected, and appropriate resolution of the cointegrate structures resulted in mutants that had lost the plasmid and in which the originalldhD was replaced by the truncated copy. These mutants completely lacked D-LDH activity. Nevertheless, the lower remaining L-LDH activity of the cells was sufficient to reroute most of the accumulating pyruvate tol -lactate. Only a marginal increase in production of the secondary end products acetaldehyde, diacetyl, and acetoin was observed. It can be concluded that inL. johnsonii D- and L-LDH are present in substantial excess for their role to eliminate pyruvate and regenerate NAD+ and that accumulated pyruvate is therefore not easily redirected in high amounts to secondary metabolic routes.

applied and environmental microbiology

<scp>d</scp> -Lactate Dehydrogenase Gene ( <i>ldhD</i> ) Inactivation and Resulting Metabolic Effects in the <i>Lactobacillus johnsonii</i> Strains La1 and N312

d -Lactate Dehydrogenase Gene ( ldhD ) Inactivation and Resulting Metabolic Effects in the Lactobacillus johnsonii Strains La1 and N312