Energy production from L-malic acid degradation and protection against acidic external pH in Lactobacillus plantarum CECT 220

García, María J.; Zúñiga, Manuel; Kobayashi, Hiroshi

doi:10.1099/00221287-138-12-2519

Cited by 15 publications

(10 citation statements)

References 26 publications

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“…Furthermore, Sheng and Marquis (44) found that L. casei had the highest specific MLF activity and the lowest pH optimum among five different species of oral LAB. More importantly, malate addition has been shown to enhance the survival of Lactobacillus plantarum and Streptococcus mutans during acid challenge at low pH values (17,44).…”

Section: Resultsmentioning

confidence: 99%

“…The electrogenic potential created by lactate efflux through a malate/lactate antiporter, whose gene is commonly organized in an operon structure with that which encodes malolactic enzyme, may also facilitate energy production (34). MLF has not been associated with the stringent response, but it has been linked to LAB survival under acidic conditions (17,34,37,44).…”

Section: Resultsmentioning

confidence: 99%

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Physiological and Transcriptional Response ofLactobacillus caseiATCC 334 to Acid Stress

et al. 2010

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This study investigated features of the acid tolerance response (ATR) inLactobacillus casei is an aciduric, rod-shaped, facultatively heterofermentative lactic acid bacterium (LAB) that can be isolated from a variety of environments including raw and fermented milk and meat or plant products, as well as the oral, intestinal, and reproductive tracts of humans and animals (24). Like other LAB species, L. casei produces lactic acid as a major end product of carbohydrate fermentation during growth, and strains of L. casei are used as acid-producing starter cultures in the preparation of fermented foods, as health-enhancing probiotic cultures, and for the production of L(ϩ)-lactic acid (18,47,52). In each of these applications, the industrial performance of L. casei strains is dependent, in one way or another, on their acidurance.During fermentation, L. casei transports lactic acid outside the cell as lactate ion via an electrogenic proton-lactate symporter. As the pH of the medium (pH o ) decreases or the concentration of lactate increases, the concentration of protonated (undissociated) lactic acid in the medium also increases. The undissociated form of lactic acid is membrane soluble and thus can enter the cytoplasm by simple diffusion (27). Metabolically active bacteria maintain a pH gradient (⌬pH) where the intracellular pH (pH i ) is more alkaline than the pH o (4, 25), so diffusion of acid into the cytoplasm results in rapid dissociation and release of protons and anions inside the cell.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Physiological and Transcriptional Response ofLactobacillus caseiATCC 334 to Acid Stress

et al. 2010

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“…casei (4,6) and Streptococcus bovis (7). Although there is evidence showing that some LAB strains can utilize lactate as a carbon source (8)(9)(10)(11)(12), most LAB cannot channel lactate into the gluconeogenic pathway. For this reason, the utilization of L-malate through MLE cannot sustain their growth, whereas the utilization of the ME pathway enables these organisms to grow with L-malate as a carbon source (3,13).…”

mentioning

confidence: 99%

Malic Enzyme and Malolactic Enzyme Pathways Are Functionally Linked but Independently Regulated in Lactobacillus casei BL23

Landete

Ferrer

Monedero

et al. 2013

Appl Environ Microbiol

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bLactobacillus casei is the only lactic acid bacterium in which two pathways for L-malate degradation have been described: the malolactic enzyme (MLE) and the malic enzyme (ME) pathways. Whereas the ME pathway enables L. casei to grow on L-malate, MLE does not support growth. The mle gene cluster consists of three genes encoding MLE (mleS), the putative L-malate transporter MleT, and the putative regulator MleR. The mae gene cluster consists of four genes encoding ME (maeE), the putative transporter MaeP, and the two-component system MaeKR. Since both pathways compete for the same substrate, we sought to determine whether they are coordinately regulated and their role in L-malate utilization as a carbon source. Transcriptional analyses revealed that the mle and mae genes are independently regulated and showed that MleR acts as an activator and requires internalization of L-malate to induce the expression of mle genes. Notwithstanding, both L-malate transporters were required for maximal L-malate uptake, although only an mleT mutation caused a growth defect on L-malate, indicating its crucial role in Lmalate metabolism. However, inactivation of MLE resulted in higher growth rates and higher final optical densities on L-malate. The limited growth on L-malate of the wild-type strain was correlated to a rapid degradation of the available L-malate to L-lactate, which cannot be further metabolized. Taken together, our results indicate that L. casei L-malate metabolism is not optimized for utilization of L-malate as a carbon source but for deacidification of the medium by conversion of L-malate into L-lactate via MLE. Lactobacillus casei is a facultatively heterofermentative lactic acid bacterium (LAB) isolated from a wide variety of habitats, including raw and fermented milk, the gastrointestinal tracts of animals, and plant materials (1). Lb. casei strains are used as cheese starter cultures, but a major interest in this species has arisen from the probiotic properties of some strains (2). Lb. casei is also remarkable because is the only LAB in which both the malic enzyme and the malolactic enzyme L-malate dissimilation pathways have been demonstrated (3, 4). Most LAB decarboxylate L-malate to L-lactate by a NAD ϩ and Mn 2ϩ -dependent malolactic enzyme (MLE). A few of them, however, can convert L-malate into pyruvate by the action of a malic enzyme (ME). This pathway was first detected in Enterococcus faecalis (5) and later in Lb. casei (4, 6) and Streptococcus bovis (7). Although there is evidence showing that some LAB strains can utilize lactate as a carbon source (8-12), most LAB cannot channel lactate into the gluconeogenic pathway. For this reason, the utilization of L-malate through MLE cannot sustain their growth, whereas the utilization of the ME pathway enables these organisms to grow with L-malate as a carbon source (3, 13).The metabolism of L-malic acid by LAB has led to considerable interest because of its relevance in winemaking (14), since the degradation of L-malate leads to a reduction in the acidity ...

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“…The electrogenic potential created by lactate efflux through a malate/lactate antiporter, whose gene is commonly organized in an operon structure with that of the malolactic enzyme, may also facilitate energy production (Poolman et al, 1991). Malate addition has been shown to enhance the survival of Lactobacillus plantarum and Streptococcus mutans during acid challenge at low pH values (García et al, 1992;Sheng and Marquis, 2007).…”

Section: 14mentioning

confidence: 99%

“…Malolactic fermentation (MLF) has been linked to lactic acid bacteria survival under acidic conditions (Renault et al, 1988;Poolman et al, 1991;García et al, 1992;Sheng and Marquis, 2007). In MLF, L-malate is decarboxylated in the cytoplasm by the malolactic enzyme to produce L-lactate and CO 2 (Renault et al, 1988).…”

Section: 14mentioning

confidence: 99%

Characterization of Two Component Systems of Lactobacillus casei BL23 and their involvement in stress response

Guarinos¹

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Energy production from L-malic acid degradation and protection against acidic external pH in Lactobacillus plantarum CECT 220

Cited by 15 publications

References 26 publications

Physiological and Transcriptional Response ofLactobacillus caseiATCC 334 to Acid Stress

Physiological and Transcriptional Response ofLactobacillus caseiATCC 334 to Acid Stress

Malic Enzyme and Malolactic Enzyme Pathways Are Functionally Linked but Independently Regulated in Lactobacillus casei BL23

Characterization of Two Component Systems of Lactobacillus casei BL23 and their involvement in stress response

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