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Lactobacilli plantarum

Landete and others (2009) reported that Lactobacillus plantarum have the ability to metabolize phenolic compounds found in olive products (such as oleuropein, hydroxytyrosol, and tyrosol, as well as vanillic, p-hydroxybenzoic, sinapic, syringic, protocatechuic, and cinnamic acids). For example, oleuropein was metabolized mainly to hydroxytyrosol, whereas protocatechuic acid was decarboxylated to catechol by the enzymatic actions. [Pg.348]

Landete JM, Curiel JA, Rodriguez H, de las Rivas B and Mufio R. 2008. Study of the inhibitory activity of phenolic compounds found in olive products and their degradation by Lactobacillus plantarum Straits. Food Chem 107(l) 320-326. [Pg.353]

The assay for pantothenic acid in whole blood, serum, urine, and cerebrospinal fluid is described here. Lactobacillus plantarum ATCC No. 8014 (formerly L. arabinosus) is used for the assay. The basal medium for assay (Table 2) is made up in double strength 2.5-ml portions of the medium are distributed into 10-ml borosilicate micro-Fembach flasks provided with aluminum caps (H18). Solutions to be assayed are added and distilled water used to bring the volume to 5 ml. The techniques for maintenance and assay are the same as those for L. casei (B12). Full growth at 37° takes 3 days. [Pg.197]

Lactobacillus plantarum is a reliable reagent for pantothenate in foods, tissues, and biologic fluids (M4, T5). It is also useful in studying the pantothenic acid content of tissues, in particular the liver. As with thiamine, the pantothenic acid levels in serum of the mother at term, although higher than in other individuals, are 5 times less than the fetus... [Pg.199]

Archibald, F. (1983). Lactobacillus plantarum, an organism not requiring iron, FEMS Microbiol. Lett., 19, 29-32. [Pg.443]

Figure 16.2 Lactobacillus plantarum Mn catalase (left) stereo view of the secondary structure— the di-Mn unit as red spheres and (right) the detailed geometry of the di-Mn centre. (From Barynin et al., 2001. Copyright 2001, with permission from Elsevier.)... Figure 16.2 Lactobacillus plantarum Mn catalase (left) stereo view of the secondary structure— the di-Mn unit as red spheres and (right) the detailed geometry of the di-Mn centre. (From Barynin et al., 2001. Copyright 2001, with permission from Elsevier.)...
Barynin, V.V., Whittaker, M.M., Antonyuk, S.V., Lamzin, V.S., Harrison, P.M., Artymiuk, PJ. and Whittaker, J.W. (2001) Crystal structure of manganese catalase from Lactobacillus plantarum,... [Pg.278]

Figure 1 Peptide pheromone structures determined by NMR. (a) Structure of peptide pheromone (PinA) from Lactobacillus plantarum required for piantaricin biosynthesis. (b) Structure of peptide pheromone (ComC) from Streptococcus pneumonia required for competence deveiopment. ... Figure 1 Peptide pheromone structures determined by NMR. (a) Structure of peptide pheromone (PinA) from Lactobacillus plantarum required for piantaricin biosynthesis. (b) Structure of peptide pheromone (ComC) from Streptococcus pneumonia required for competence deveiopment. ...
Peptide Signaling Regulation of Carbohydrate Metabolism in Lactobacillus plantarum... [Pg.316]

CASRN 115-90-2 molecular formula CnHi704PS2 FW 308.35 Soil. In soils, the bacterium Klebsiella pneumoniae degraded fensulfothion to fensulfothion sulfide (Timms and MacRae, 1982, 1983). The following microorganisms were also capable of degrading the parent compound to the corresponding sulfide Escherichia coli. Pseudomonas Huorescens, Nocardia opaca, Lactobacillus plantarum, and Leuconostoc mesenteroides (Timms and MacRae, 1983). [Pg.1583]

Lactobacillus bulgaricus Lactobacillus plantarum Streptococcus cremoris Streptococcus lactis... [Pg.95]

Crystal structures of manganese catalases (in the (111)2 oxidation state) from Lactobacillus plantarum,its azide-inhibited complex, " and from Thermus thermophilus have been determined. There are differences between the structures that may reflect distinct biological functions for the two enzymes, the L. plantarum enzyme functions only as a catalase, while the T. thermo-philus enzyme may function as a catalase/peroxidase. The active sites are conserved in the two enzymes and are shown schematically in Figure 32. Each subunit contains an Mu2 active site,... [Pg.100]

Rooke, J.A., Borman, A.J. and Armstrong, D.G. (1990) The effect of inoculation with Lactobacillus plantarum on fermentation... [Pg.217]

Lactobacillus plantarum, 33 214 Lactoferrin, 41 390 anion sites, 41 418 biological role, 41 392-393... [Pg.158]

Z0285 Nes, I. E., R. Skjelkvale, O. Olsvik, and Z0296 B. P. Berdal. The effect of natural spices and oleoresins on Lactobacillus plantarum and Staphylococcus aureus. [Pg.557]

III) form of Lactobacillus plantarum is depicted in Fig. 13 [105,106]. The Mn centers are bridged by oxo, hydroxo, and car-boxylato ligands in a manner similar to the binuclear structures (8-10) in Sect. 16.1.4. A proposed mechanism for hydrogen peroxide dismutation by Mn catalase is presented in Fig. 14. A number of model studies of H2O2 disproportionation employing bridged binuclear Mn complexes have been conducted [107]. [Pg.423]

Fig. 13 A schematic drawing of the active site of manganese catalase from Lactobacillus plantarum (reprinted from Ref 105, Copyright 2003 with permission from Elsevier). Fig. 13 A schematic drawing of the active site of manganese catalase from Lactobacillus plantarum (reprinted from Ref 105, Copyright 2003 with permission from Elsevier).
Kleerebezem, M. Boekhorst, J. van Kranenburg, R. et al. Complete genome sequence of Lactobacillus plantarum WCFSl. Proc. Natl. Acad. Sci. USA, 100, 1990-1995 (2003)... [Pg.455]

Diep, D.B. Havarstein, L.S. Nissen-Meyer, J. Nes, LE The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum Cll, is located on the same transcription unit as an agr-like regulatory system. Appl. Environ. Microbiol., 60, 160-166 (1994)... [Pg.456]

The possibility now arises that if, in fact, there is an intermediate involved in the conversion of malic acid to lactic acid, the cell may, in some way, be capable of deriving energy from it. In 1950, Korkes et ah (14), working with the malo-lactic system of Lactobacillus plantarum, demonstrated the production of a very small amount of pyruvic acid (0.2% ) from malic acid. However, 98% of the malic acid was recovered in lactic acid, and the recovery of carbon dioxide was consistent with conversion of 90% of the malic acid. The pyruvic acid recovery was attributed to spillage from the enzyme surface. We will see below that a small amount of pyruvic acid and NADH are indeed produced during... [Pg.180]


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