Lactobacillus casei

A number of deaza analogs of pteroic acid (182, Ri = R2 = OH) have been prepared and examined by Rydon el al. as antagonists of folic acid in Streptococcus faecalis and Lactobacillus casei. Two of the pyrido[3,2-d]pyrimidines (183, R = OH or OEt, R2 = NH2) showed... 

Matthews DA, Alden RA, Bolin JT, Filman DJ, Freer ST, Hamlin R, Hoi WG, Kisliuk RL, Pastore EJ, Plante FT, Xuong N, Kraut J. Dihydrofolate reductase from Lactobacillus casei. X-ray structure of the enzyme methotrexate-NADPH complex. J Biol Chem 1978 253 6946-54. 

Bees and ants are not the only critters that attack using acid. Bacteria, such as those found in plaque, do, too. Saliva usually keeps the mouth at a pH of about 6.8. Any pH of 6.0 or higher does not cause the teeth any problems. Plaque, a bacteria-containing film that builds up on teeth, can cause that pH to plummet. That is because it contains bacteria such as Streptococcus mutans, Lactobacillus casei, and Lactobacillus acidophilus that feed on sugars and make lactic acid. These conditions can lower the pH in the mouth to 5.5 or less. 

Bautista-Garfias, C.R., Ixta, O., Orduna, M., Martinez, F., Aguilar, B. and Cortes, A. (1999) Enhancement of resistance in mice treated with Lactobacillus casei effect on Trichinella spiralis infection. Veterinary Parasitology 80, 251-260. 

Koebnick C, Wagner I, Leitzmann P, Stem U, Zunft HJ Probiotic beverage containing Lactobacillus casei Shirota improves gastrointestinal symptoms in patients with chronic constipation. Can J Gastroenterol 2003 17 655-659. 

Lactobacillus casei TISTR 1500 Methyl Orange The complete decolorization of the dye was achieved in 2.5 h [75]... 

Methyl Orange, Methyl Red Lactobacillus casei TISTR 1500 0.23 mmol L-1 6.1-31.0 [75]... 

Seesuriyachan P, Takenaka S, Kuntiya A (2007) Metabolism of azo dyes by Lactobacillus casei TISTR 1500 and effects of various factors on decolorization. Wat Res 41 985-992... 

Crystal structures of escherichia coli and lactobacillus casei dihydrofolate reductase refined at 1.7A resolution, J. Biol. Chem. 257 13663 (1982). 

Hoi, R. L. Kisliuk, E. J. Pastore, L. T. Plante, N. Xuong, J. Kraut, Dihydrofolate reductase from lactobacillus casei, J. Biol. Chem. 253 6946 (1978). 

Refined structures of substrate-bound and phosphate-bound thymidylate synthase from lactobacillus casei, J. Mol. Biol. 232 1101 (1993). 

A variety of biotin-requiring microorganisms have been used to assay biotin Saccharomyces cerevisiae (H6), Lactobacillus casei (S2), Lactobacillus arabinosus (now L. plantarum ATCC No. 8014) (W14), Micrococcus sodonensis (Al), Neurospora crassa (H10), and Rhizobium tri-folii (W7). None have been applied successfully for assaying biotin in biologic fluids. Because the flagellate Ochromoms danica had a specific and sensitive biotin requirement (A2), it was utilized as a reagent for biotin in blood, serum, urine, brain, and liver tissue (B3b). 

Nearly all microbiologic assays for folic acid activity have used Streptococcus faecalis and Lactobacillus casei. Earlier it appeared that these organisms could not detect folic acid deficiency in man (C2, L8) for example, in one study using S. faecalis there was no detectable activity in the fasting serum of humans (C3). Administration of a loading dose of folic acid with subsequent assay by S. faecalis (G9) has served as a workable means of determining folic acid deficiency (C6), a technique having definite drawbacks (G10). 

Sivakesava et al. also used Raman (as well as FT-IR and NIR) to perform a simultaneous on-line determination of biomass, glucose, and lactic acid in lactic acid fermentation by Lactobacillus casei.2 Partial least squares (PLS) and principal components regression (PCR) equations were generated after suitable wavelength regions were determined. The best standard errors were found to be glucose, 2.5 g/1 lactic acid, 0.7 g/1 and optical cell density, 0.23. Best numbers were found for FT-IR with NIR and Raman being somewhat less accurate (in this experiment). 

Hudault, S., Lievin, V., Bernet-Camard, M. F., and Servin, A. L. (1997). Antagonistic activity exerted in vitro and in vivo by Lactobacillus casei (strain GG) against Salmonella typhimurium C5 infection. Appl. Environ. Microbiol. 63, 513-518. 

The expansion in the power of computers and theoretical methods has made it possible to investigate the mechanism of action of enzymes by combinations of quantum-mechanical and molecular-mechanical calculations. A study of two possible mechanisms for dihydrofolate reductase catalysis was consistent with indirect proton transfer from aspartate to N-5 of the pterin as has been suggested for many years by crystallographic evidence <2003PCB14036>. This conclusion is also consistent with the outcome of a study that directly measured the of the active site aspartate in the Lactobacillus casei enzyme <1999B8038>. Observations of chemical shifts of... 

Knappe J, Briiminer W, Biederbick (1963) Reinigung und Eigenschaften der Biotinidase aus Schweinenieren und Lactobacillus casei. Biochem Z 338 599-613... 

Studies on growth factors required by certain microorganisms, for example Streptococcus faecalis and Lactobacillus casei, and of their relevance in animal nutrition, led to the isolation and characterization of folic acid, pteroylglutamic acid (104), the structure of which was determined in 1946. It is an essential vitamin for man and together with vitamin B12 it is involved in the development of blood cells. Deficiency causes macrocytic anaemia. Many microorganisms do not use exogenous folic acid, but synthesize their own, and some... 

A cheese-like spread, which is similar to processed cheese spread, is prepared by combining hydrolyzed Swiss-or Cheddar-whey protein and cultured cream. The whey protein is precipitated by heat and acid. The granular, chalky precipitate then acquires a smooth texture by enzymatic hydrolysis with Rhozyme P-11 at 39.5 to 40.5 °C for 30 min. The product is heated to 85 °C for 15 min to inactivate the enzymes then it is homogenized and blended with an equal quantity of 45° cream culture containing Lactobacillus casei (Webb and Whittier 1970). 

Brandsaeter, E. and Nelson, F. E. 1956A. Proteolysis by Lactobacillus casei. I. Proteinase activity. J. Bacteriol. 72, 68-72. 

Chassy, B. M. and Thompson, J. 1983. Regulation of lactose-phosphoenolpyruvate-dependent phosphotransferase system and 0-D-phosphogalactoside galactohydrol-ase activities in Lactobacillus casei. J. Bacteriol 154, 1195-1203. 

El Soda, M., Bergere, J. L. and Desmazeaud, M. J. 1978A. Detection and localization of peptide hydrolases in Lactobacillus casei. J. Dairy Res. 5, 519-524. 

Hensel, R., Mayr, R., Stetter, K. 0. and Kandler, O. 1977. Comparative studies of lactic acid dehydrogenase in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei spp. casei and, Lactobacillus curvatus. Arch. Microbiol 112, 81-93. 

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