Peroxidases waters

Cooper VA, Nicell JA. Removal of phenols from a foundry wastewater using horseradish peroxidase. Water Res 1996 30(4) 954-964. 

Caza N, Bewtra JK, Biswas N et al (1999) Removal of phenolic compounds from synthetic wastewater using soybean peroxidase. Water Res 33 3012-3018... 

Place about o-i g. (or 0 1 ml.) of the amine in a test-tube, add o-i ml. of glacial aatic acid to dissolve the amine and then add water until the test-tube is half-full Next place about 0 3 g. of the peroxidase preparation in a very small mortar and grind up with about 15 ml. of water. Filter through a small fluted filter-paper into a test-tube. 

Yan J. Wang J. Tissue D. Holaday A. S. Allen R. Zhang H. (2003) Protection of photosynthesis and seed production under water-deficit conditions in transgenic tobacco plants that over-express Arabidopsis ascorbate peroxidase // Grop Sci. V. 43. P. 1477-483. 

FIGURE 9.11 Relative mass change as a result of water absorption and loss in a solid piece of recombinant resilin prepared from a 20% protein solution in phosphate-buffered sahne (PBS), cross-linked using peroxidase (see [29] supplementary material). The fuUy swollen sample is designated 100. (Data courtesy of Shekibi, Y., Naim, K., Bastow, T.J., and HiU, A.J., The states of water in a protein based hydrogel. Internal CSIRO... 

In hiphasic water/1L mixtures, the latter can he used as immohilization systems. This idea was used for the synthesis of conducting polyanihne hy IL-immohilized horseradish peroxidase [68]. Tuning the IL hydrophohicity hy changing the anionic component allowed the increase in the yield of the product hy altering the affinity of the product to the IL. After completion of the reaction, the IL phase was separated, facilitating the recovery of the enzyme. 

Okrasa and co-workers reported an interesting combination reaction of glucose oxidase and peroxidase in a mixed solvent of [bmimJpFg] with water (Fig. 18). Asymmetric oxidation of sulfide was accomplished successfully in the reaction system. ... 

Thiols are also important protection against lipid peroxidation. Glutathione (7-Glu-Cys-Gly) is used by several glutathione-dependent enzymes such as free-radical reductase (converts vitamin E radical to vitamin E), glutathione peroxidase (reduces hydrogen peroxide and lipid hydroperoxides to water and to the lipid alcohol, respectively), and others. In addition, the thiol group of many proteins is essential for function. Oxidation of the thiol of calcium ATPases impairs function and leads to increased intracellular calcium. Thiol derivatives such as the ovothiols (l-methyl-4-mercaptohistidines) (Shapiro, 1991) have been explored as therapeutics. 

Catalase and Peroxidase are produced inside the microbes and will be located in the cell wall. When these cells pass away either due to age or due to external circumstances their content will spread out in the water. These free-swimming molecules of Catalase are the worst due to that HP have the best accessibility to them, the reaction could not be faster. 

Figure 4 Stabilized bromine antimicrobials are produced by eosinophils, a type of mammalian white blood cell. Bacteria are captured by phagocytosis and contained intracellularly within vesicles called phagosomes. Granules release cationic surfactants, lytic enzymes, and eosinophil peroxidase into the phagosome in a process known as degranulation. Eosinophil peroxidase, an enzyme that is structurally similar to the bromoperoxidases found in seaweed (Figure I), selectively catalyzes oxidation of bromide to hypobromite by reducing hydrogen peroxide to water. The hypobromite immediately reacts with nitrogenous stabilizers such as aminoethanesulfonic acid (taurine) to form more effective and less toxic antimicrobial agents.

Zhang, G. and Nicell, J.A., Treatment of aqueous pentachlorophenol by horseradish peroxidase and hydrogen peroxide, Water Res., 34, 1629-1637, 2000. 

Wondrack, L. Szanto, M., and Wood, W. A., Depolymerization of Water-Soluble Coal Polymer from Subbituminous Coal and Lignite by Lignin Peroxidase. Applied Biochemistry and Biotechnology, 1989. 20-1 pp. 765-780. 

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