The effect of oxygen and pH on the glucose metabolism ofLactobacillus casei var.rhamnosus ATCC 7469

Manderson, G. J.; Doelle, Horst W.

doi:10.1007/bf02328095

Cited by 12 publications

(9 citation statements)

References 38 publications

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“…In general, when C4 compounds accumulate in growing cultures pyruvate, or an alternative source of pyruvate such as citrate, is available in addition to the fermentable sugar [54,78,[80][81][82][83]. Neverthe- less, C4 compounds have been observed occasionally in cultures of some streptococci growing in a sugar-based medium without additional pyruvate [41,73,79,84,85].…”

Section: Transformation Of Pyruvate To Acetoin 23butanediol and Diamentioning

confidence: 99%

Responses of lactic acid bacteria to oxygen

Condón

1987

FEMS Microbiology Letters

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Key words: Lactic acid bacteria; Oxygen SUMMARY 2. INTRODUCTIONA small number of flavoprotein oxidase enzymes are responsible for the direct interaction of lactic acid bacteria (LAB) with oxygen; hydrogen peroxide or water are produced in these reactions. In some cultures exposed to oxygen, hydrogen peroxide accumulates to inhibitory levels.Through these oxidase enzymes and NADH peroxidase, 02 and H202 can accept electrons from sugar metabolism, and thus have a sparing effect on the use of metabolic intermediates, such as pyruvate or acetaldehyde, as electron acceptors. Consequently, sugar metabolism in aerated cultures of LAB can be substantially different from that in unaerated cultures. Energy and biomass yields, end-products of sugar metabolism and the range of substrates which can be metabolised are affected.Lactic acid bacteria exhibit an inducible oxidative stress response when exposed to sublethal levels of H202. This response protects them if they are subsequently exposed to lethal concentrations of H202. The effect appears to be related to other stress responses such as heat-shock and is similar, in some but not all respects, to that previously reported for enteric bacteria.

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Section: Transformation Of Pyruvate To Acetoin 23butanediol and Diamentioning

confidence: 99%

Responses of lactic acid bacteria to oxygen

Condón

1987

FEMS Microbiology Letters

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“…However, Christensen and Pederson (4) reported that homofermentative but not heterofermentative lactic acid bacteria produced increased levels of diacetyl when citrate was added to the medium. In addition, several workers have reported acetoin and/or diacetyl production by lactobacilli in media containing either citrate or malate, but whether the acids were being utilized simultaneously during growth was not measured (2,4,7,8,15,18). Citrate utilization appears to be widespread among lactobacilli as Fryer (10) reported that 19 out of 25 strains of Lactobacillus casei, Lactobacillus plantarum, and Lactobacillus brevis utilized citrate in the presence of a fermentable carbohydrate.…”

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Citric acid metabolism in hetero- and homofermentative lactic acid bacteria

Drinan¹,

Robin²,

Cogan³

1976

Appl Environ Microbiol

103

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The effect of citrate on production of diacetyl and acetoin by four strains each of heterofermentative and homofermentative lactic acid bacteria capable of utilizing citrate was studied. Acetoin was quantitatively the more important compound. The heterofermentative bacteria produced no acetoin or diacetyl in the absence of citrate, and two strains produced traces of acetoin in its presence. Citrate stimulated the growth rate of the heterofermentative lactobacilli. Acidification of all heterofermentative cultures with citric acid resulted in acetoin production. Destruction of accumulated acetoin appeared to coincide with the disappearance of citrate. All homofermentative bacteria produced more acetoin and diacetyl in the presence of citrate than in its absence. Citrate utilization was begun immediately by the streptococci but was delayed until at least the middle of the exponential phase in the case of the lactobacilli.

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“…The ability of L.casei to produce more lactate at acid pH values [12,50] lead deVries and co-workers to suggest that the intracellular concentration of fructose 1,6-bisphosphate could determine the quantity of pyruvate to be converted to lactate. A scheme for the regulation of glucose carbon flow between the Embden-Meyerhof-Parnas and hexose-inonophosphate pathways based on the fructose 1,6-bisphosphate activation of lactate dehydrogenase in S. fuecalis has therefore been proposed [51].…”

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Purification, Properties and Immunological Relationship of l(+)‐Lactate Dehydrogenase from Lactobacillus casei

Gordon

Doelle

1976

European Journal of Biochemistry

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The fructose-1,6-bisphosphate-activated L-lactate dehydrogenase (EC 1.1 .I .27) from Lactobacillus casei ATCC 393 has been purified to homogenity by including affinity chromatography (cibacronblue -Sephadex-G-200) and preparative polyacrylamide gel electrophoresis into the purification procedures. The enzyme has an M , of 132000-135000 with a subunit M , of 34000. The pH optimum was found to be 5.4 in sodium acetate buffer. Tris/maleate and citrate/phosphate buffers inhibited enzyme activity at this pH. The enzyme was completely inactivated by a temperature increase from 60 "C to 70 "C. Pyruvate saturation curves were sigmoidal in the absence of fructose 1,6-bisphosphate. In the presence of 20 pM fructose 1,6-bisphosphate a K, of 1 .OmM for pyruvate was obtained, whereas fructose 1,6-bisphosphate had no effect on the K,,, of 0.01 mM for NADH. The use of pyruvate analogues revealed two types of pyruvate binding sites, a catalytic and an effector site. The enzyme from L. casei appears to be subject to strict metabolic control, since ADP, ATP, dihydroxyacetone phosphate and 6-phosphogluconate are strong inhibitors.Immunodiffusion experiments with a rabbit antiserum to L. casei lactate dehydrogenase revealed that L. casei ATCC 393 L( +)-lactate dehydrogenase is probably not immunologically related to group D and group N streptococci. Of 24 lactic acid bacterial strains tested only 5 strains did cross-react :Fructose 1,6-bisphosphate activation of lactate dehydrogenase is found widely in several streptococcal groups [I -61. This phenomenon also exists among bifidobacteria [7], fermentative mycoplasmas [S, 91, certain coagulase-negative and mannitol-negative staphylococci [lo], and an actinomycete [l 11. However, Lactobacillus casei is the only member of its genus which possesses a fructose-l,6-bisphosphate-activated lactate dehydrogenase [12,32], with the enzyme being specific for L(+)-lactate [12]. This lactate isomer is also the major end-product of glucose fermentation [13]. Immunological and hence evolutionary links have been established between the isofunctional malic enzyme from Streptococcus fuecalis and L. cusei [14, 151. Further evidence of a close relationship between these two genera was obtained [16] using an antiserum prepared from purified S. faecalis fructose-l,6-bisphosphate aldolase. Difficulties in assaying and purifying L. casei lactate dehydrogenase [17] precluded this lactic acid bacterium from an immunological study of the relationships among lactate dehydrogenase from lactobacilli and leuconostocs [18].The presented paper reports the purification of L( +)-lactate dehydrogenase from L. casei to a homogenous preparation and establishes the kinetic characteristics of this enzyme. It also investigates the effects of various divalent metal ions, reaction products, metabolic intermediates and adenylates in an effort to elucidate the metabolic control of glucose utilization as well as the immunological relationship to the lactate dehydrogenases of other lactic acid bacteria.

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The effect of oxygen and pH on the glucose metabolism ofLactobacillus casei var.rhamnosus ATCC 7469

Cited by 12 publications

References 38 publications

Responses of lactic acid bacteria to oxygen

Responses of lactic acid bacteria to oxygen

Citric acid metabolism in hetero- and homofermentative lactic acid bacteria

Purification, Properties and Immunological Relationship of l(+)‐Lactate Dehydrogenase from Lactobacillus casei

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