Peroxidase activity

Tussen, R, and Kurstak, E. (1984) Highly efficient and simple methods for the preparation of peroxidase and active peroxidase—Antibody conjugates for enzyme immunoassays. Anal. Biochem. 136, 451-457. 

Nazari K, Esmaeili N, Mahmoudi A, Rahimi H and Moosavi-Movahedi AA. 2007. Peroxidative phenol removal from aqueous solutions using activated peroxidase biocatalyst. Enz Microb Technol 41 226-233. 

Estimated in the oxidation of 2,3,5,6-tetrachlorophenol Estimated in the oxidation of pentachlorophenol Estimated in the oxidation of 2,3,5,6-tetrachloroaniline Estimated in the presence of H202 Estimated in the presence of H202 Estimated in the presence of H202 Monooxygenase activity Peroxidase activity Parameters obtained from Hill equation where Km = Ku and n = 2.03 Oxidation reaction in the presence of H202 Oxidation of parathion Oxidation of styrene in ternary solvent mixtures in the presence of 200 mM of /-butyl hydroperoxide [46] [53] [53] [53] [53] [53] [53] [46] [54] [54] [55] [56] [56] [57]... 

Xie, Yuchun, Das, Prasanta Kumar, Klibanov, Alexander M. (2001) Excipients activate peroxidases in specific but not in non-specific reactions in organic solvents, Biotechnology Letters 23, 1451-1454. 

Collect the brown fractions, which contain the activated peroxidase, pool, and concentrate to 1 ml. 

Glycosidase enzymes can be very destructive of anthocyanins, but their source is unlikely to be the berries themselves. Moldy fruit is a potential source (Rwabahizi and Wrolstad, 1988) as are commercial juice-processing pectolytic enzyme preparations that may have glycosidase side activities (Wrolstad et al., 1994). Native peroxidase enzymes may be a cause of anthocyanin destruction in some berry commodities. Active peroxidase may be a major contributor to anthocyanin pigment destruction in many processed strawberry products (Lopez-Serrano and Ros Barcelo, 1996 Zabetakis et al., 2000). 

Catesson, A. M., A. Pang, and R. Goldberg Use of cytochemical techniques for the detection of cell wall enzyme activities Peroxidases Actual. Botany (1991) 257-262. 

Tranylcypromine, a monoamine oxidase inhibitor also inhibits prostacyclin synthetase in vitro (IC50 = 160 jig/m ) [96]. This is much weaker than the inhibition induced by the fatty acid hydroperoxides (IC50 = 0.5 /xg/ml) [85]. Fortunately, the latter products are not active when administered in vivo due to active peroxidases which reduce the hydroperoxides to the inactive hydroxides. Other inhibitors of prostacyclin synthesis are the endoperoxide analogs (9,11-diaza and 9,11-epoxyimino-prosta-5,13-dienoic acid) [97] and an indole hydroperoxide [98]. 

Most lactic acid bacteria tolerate the presence of oxygen but do not use it in energy-producing mechanisms. Depending on the species, they use different pathways to eliminate the toxic peroxide, activating peroxidases which use NADH as a reducer a superoxide dismutase, a pseudo catalase and sometimes Mn + ions (Desmazeaud and Roissart, 1994). To date, this subject has not been specifically studied for species isolated in wine. 

Manganous ions activate peroxidase as an oxidase toward oxalate, oxalacetate, ketomalonate, and dihydroxytartrate. A peroxidase substrate is necessary for the reaction with the first two substrates, but not for the last two. These reactions depend upon the presence of peroxide. They can be facilitated by adding peroxide, or inhibited by adding catalase, but it is uncertain whether they are instances of direct oxidase action, or of peroxidatic activity (414). 

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