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[Thermostabilities of plant phenol oxidase and peroxidase, determining the technology of their use in food industry].

Stabilities of phenol oxidase and peroxidase from tea plant (Camellia sinensis L.) clone Kolkhida leaves, apple (Malus domestica L.) cultivar Kekhura fruits, walnut (Juglans regia L.) green pericarp, and horseradish (Armoracia lapathifolia Gilib) roots were studied using different storage temperature modes and storage duration. It was demonstrated that both enzymes retained residual activities (approximately 10%) upon 20-min incubation at 80 degrees C. Phenol oxidases from tea, walnut, and, especially, apple, as well as tea peroxidase were stable during storage. A technology for treatment of plant oxidases was proposed, based on the use of a natural inhibitor phenol oxidase and peroxidase, isolated from tea leaves, which solving the problem of residual activities of these enzymes, arising during pasteurization and storage of beverages and juices. It was demonstrated that browning of apple juice during pasteurization and beer turbidity during storage could be efficiently prevented using the natural inhibitor of these enzymes.

Enzyme Stability↗
PubMed1985

Inactivation of Escherichia coli glutamine synthetase by xanthine oxidase, nicotinate hydroxylase, horseradish peroxidase, or glucose oxidase: effects of ferredoxin, putidaredoxin, and menadione.

Previous studies have shown that several mixed-function oxidation (MFO) systems are capable of catalyzing the inactivation of glutamine synthetase (GS) [R.L. Levine, C. N. Oliver, R. M. Fulks, and E. R. Stadtman (1978) Proc. Natl. Acad. Sci. USA 78, 2120-2124] and a number of the other enzymes [L. Fucci, C. N. Oliver, M. J. Coon, and E. R. Stadtman (1983) Proc. Natl. Acad. Sci. USA 80, 1521-1525]. It has now been found that in the presence of Fe(III), O2, and an appropriate electron donor (hypoxanthine or NADPH, respectively) glutamine synthetase is also inactivated by either milk xanthine oxidase or Clostridial nicotinate hydroxylase. Inactivation of glutamine synthetase by either of these flavoproteins is greatly stimulated by the presence of electron carrier proteins possessing nonheme-iron-sulfur (NHIS) clusters (i.e., ferredoxin or putidaredoxin) or by the presence of menadione. The inactivation reactions are partially inhibited by free radical scavengers, superoxide dismutase, (SOD), histidine, mannitol, dimethyl sulfoxide, and dimethylthiourea, and are inhibited completely by either Mn(II), EDTA, or catalase. The sensitivity to SOD inhibition is greatly suppressed when the xanthine oxidase system is supplemented with either ferredoxin or redoxin. In the presence of the latter NHIS-proteins (and only when they are present), MFO systems, comprised of either horseradish peroxidase and H2O2 or glucose oxidase, O2, and glucose, can also catalyze the inactivation of GS. The ability of ferredoxin and putidaredoxin to promote oxidation modification of GS by any one of these MFO systems suggests that proteins with NHIS centers may mediate the generation (or stabilization) of highly reactive radical intermediates.

Adenosine Diphosphate↗
PubMed1996

Changes in phenol oxidase and peroxidase levels in cocoyam tubers of different postharvest ages infected by Sclerotium rolfsii sacc.

Crude aqueous extracts from the peripheral rot zone of cocoyam tubers infected by Sclerotium rolfsii sacc were shown to be inhibitory to dialysed in vivo polygalacturonase (PG) of the pathogen. The PG inhibitory action, phenol oxidase and peroxidase activities were higher in cocoyam tubers of the Xanthosoma sagittifolium varieties than in those of the Coolocasia esculenta varieties. The levels of phenol oxidase, peroxidase and PG inhibitory activities also decreased as the postharvest age of the tubers increased.

Food Contamination↗
PubMed1996

Entrapment of both glucose oxidase and peroxidase in regenerated silk fibroin membraneCharacterization of the membrane structure and its application to an amperometric glucose sensor employing methylene green as an electron transfer mediato.

Two enzmyes, glucose oxidase and peroxidase, were for the first time simultaneously immobilized in regenerated silk fibroin membrane. The structure and morphology of the regenerated silk fibroin membrane containing both glucose oxidase and peroxidase were investigated with IR spectra and SEM. The bienzymes do not change the structures of the regenerated silk fibroin in the membrane, which has an islands-sea structure. For the first time, an amperometric methylene green mediating sensor for glucose based on co-immobilization of both glucose oxidase and peroxidase in regenerated silk fibroin was constructed. Cyclic voltammetry and amperometry were used to test the suitability of methylene green shuttling electrons between peroxidase and the glassy carbon electrode. The bienzyme-based system offers fast response and high sensitivity of the sensor to glucose. The effects of pH, temperature, and the concentration of the mediator on the response current were evaluated, and the dependence of the Michaelis-Menten constant K(m)(app) on the concentration of the mediator was investigated.

Journal Article↗
PubMed1990

In vitro oxidation of indoleacetic Acid by soluble auxin-oxidases and peroxidases from maize roots.

Soluble auxin-oxidases were extracted from Zea mays L. cv LG11 apical root segments and partially separated from peroxidases (EC 1.11.1.7) by size-exclusion chromatography. Auxin-oxidases were resolved into one main peak corresponding to a molecular mass of 32.5 kilodaltons and a minor peak at 54.5 kilodaltons. Peroxidases were separated into at least four peaks, with molecular masses from 32.5 to 78 kilodaltons. In vitro activity of indoleacetic acid-oxidases was dependent on the presence of MnCl(2) and p-coumaric acid. Compound(s) present in the crude extract and several synthetic auxin transport inhibitors (including 2,3,5-triiodobenzoic acid and N-1-naphthylphthalamic acid) inhibited auxin-oxidase activity, but had no effect on peroxidases. The products resulting from the in vitro enzymatic oxidation of [(3)H] indoleacetic acid were separated by HPLC and the major metabolite was found to cochromatograph with indol-3yl-methanol.

Journal Article↗
PubMed1993

Virucidal effects of glucose oxidase and peroxidase or their protein conjugates on human immunodeficiency virus type 1.

Glucose oxidase and peroxidase (lactoperoxidase or myeloperoxidase) are virucidal to human immunodeficiency virus type 1 (HIV-1) in the presence of sodium iodide, as assessed by the loss of viral replication in a syncytium-forming assay or by the inhibition of cytopathic effects on infected cells. In the presence of low concentrations of sodium iodide, five HIV-1 isolates were equally susceptible to this virucidal system at enzyme concentrations of a few milliunits. The loss of viral replication was linearly related to the time of incubation in the enzyme solutions, with an inactivation rate of 1 log unit every 30 min. These enzymes and this halide were also cytotoxic to chronically infected, but not to uninfected, cultured CEM cells. Protein conjugates were prepared by using the enzymes and murine antibody 105.34, which recognized the V3 loop of HIV-1 LAI isolate surface glycoprotein, or recombinant human CD4. The protein conjugates inactivated free virus at rates similar to those of the free enzymes and were more effective than antibody or recombinant CD4 alone. These in vitro findings demonstrate that the peroxidase-H2O2-halide system provides potent virucidal activity against HIV-1.

Antibodies, Monoclonal↗
PubMed2000

Involvement of diamine oxidase and peroxidase in insolubilization of the extracellular matrix: implications for pea nodule initiation by Rhizobium leguminosarum.

Rhizobium leguminosarum colonizes host cells and tissues through infection threads, which are tubular in-growths of the plant cell wall. Monoclonal antibody MAC265 recognizes a plant matrix glycoprotein (MGP) associated with the lumen of these infection threads. This glycoprotein is also released in soluble form from the root tips of pea seedlings. In the presence of hydrogen peroxide, release of glycoprotein from root tips was not observed. Extractability from root tips was therefore used as the basis for investigating the peroxide-driven insolubilization of MGP and the possible involvement of two extracellular enzymes, peroxidase (POD) and diamine oxidase (DAO), was investigated. Release of MGP from root tips was enhanced by application of POD and DAO inhibitors (salicylhydroxamic acid and o-phenanthroline, respectively). Furthermore, release of MGP was inhibited by pretreatment of roots with putrescine (the substrate of DAO) and also by application of a partially purified extract of DAO from pea shoots. Following inoculation of pea roots with R. leguminosarum, elevated levels of DAO transcript were observed by reverse transcriptase-polymerase chain reaction (RT-PCR), but these then dropped to a low level from 4 to 10 days post inoculation, rising again in more mature nodules. In situ hybridization studies indicated that the bulk of the transcription was associated with the infected tissue in the center of the nodule. On the basis of these observations, we postulate that DAO may be involved in the peroxide-driven hardening of MGP in the lumen of infection threads and in the intercellular matrix.

Amine Oxidase (Copper-Containing)↗
PubMed1978

The role of certain oxidative enzymes, catalase, and beta-glucosidase on virulence of Cephalosporium maydis.

Isolates of Cephalosporium maydis varied in their pathogenicity to D.C. 67 maize cultivar from highly to weakly pathogenic. Highly pathogenic isolates showed lower activity of polyphenol oxidase, peroxidase, cytochrome oxidase, and beta-glucosidase enzymes and higher activity of catalase and dehydrogenase than weakly pathogenic isolates. Enzymes production by the tested isolates increased as the culture age increased; except in case of catalase enzyme, the reverse action was detected. The role of these enzymes in the virulence of C. maydis is suggested and discussed.

Acremonium↗
PubMed2002

Biotransformation of d-limonene to carvone by means of glucose oxidase and peroxidase.

A novel method for enzymatic biotransformation of limonene to carvone has been developed. It involves addition glucose oxidase and peroxidase to the biotransformation medium. Some factors affecting biotransformation yield were investigated. Maximal yield of carvone occurred in the medium containing 1.5% substrate, at 50 degrees C and pH 7.0.

Biotransformation↗
PubMed2000

Kinetic studies and analytical application of cholesterol oxidase and peroxidase immobilized to synthetic polymer.

A method for individual and simultaneous covalent immobilization of cholesterol oxidase and peroxidase to copolymer of acrylonitrile with acrylamide is described. The effect of immobilization on the catalytic properties of the covalently bound enzymes was studied. The immobilized enzymes showed no change in pH optima and an increase in temperature optima, activation energy, and Km' compared to data received from experiments with soluble enzymes. A small glass column packed with immobilized multienzyme complex was used to develop a method for manual determination of cholesterol in foodstuffs (e.g., in mayonnaise "Olinease"). The method was characterized by high analytical precision (coefficient of variation = 2.67%). The results show high correlation with those obtained by the Kageyama method (r = 0.986). The method is economical (the enzyme-carrier conjugate may be used more than 300 times), precise, easy to perform, and less time-consuming than the manual methods utilizing soluble enzymes. The established manual method can be proposed for cholesterol determination in foodstuffs.

Acrylamide↗
PubMed1969

Studies on polyphenol content, activities and isozymes of polyphenol oxidase and peroxidase during air-curing in three tobacco types.

The change in polyphenol content in the primed leaves of burley, flue-cured, and Turkish tobaccos during air-curing was related to the activities and isozymes of polyphenol oxidase and peroxidase. The quantity of chlorogenic acid was rapidly reduced during the first week of curing. The decrease in rutin content during curing was less significant, especially when the concentration of chlorogenic acid was high in leaf tissues. This result was further confirmed by in vitro assays with partially purified tobacco polyphenol oxidase.The polyphenol oxidase activity did not differ at any stage of curing in the 3 tobaccos. When the activity was measured by the oxidation of 3,4-dihydroxyphenylalanine it rose rapidly during the first day of curing and then decreased sharply so that in the fully cured leaf only 15% activity remained. The increase in activity was not observed when chlorogenic acid was used as the substrate. A similar level of peroxidase activity was found in the 3 tobaccos before curing. Peroxidase activities increased rapidly during the first 24 hr of curing, declined thereafter, and remained highest in the flue-cured tobacco, less in the Turkish line, and least in the burley at the end of curing process.By polyacrylamide gel block electrophoresis, 10 peroxidase isozyme bands, 2 cationic and 8 anionic, appeared identical in all 3 tobaccos. When catechol replaced benzidine-2 HCl as the electron donor, 1 cationic and 2 anionic peroxidase isozymes did not form. Of interest is that the same 10 peroxidase isozyme bands also exhibited polyphenol oxidase activities when treated with 3,4-dihydroxyphenylalanine or chlorogenic acid. Results suggest that in the crude tobacco leaf extract the peroxidase and polyphenol oxidase may associate as protein complexes, and peroxidase isozymes may differ in electron-donor requirements. Isozyme patterns for both oxidases at various curing intervals differed only quantitatively.

Journal Article↗
PubMed1976

Measurement of glucose in plasma, with use of immobilized glucose oxidase and peroxidase.

We describe a novel fluorometric technique for simple, rapid, and economical assay of glucose by use of immobilized glucose oxidase and peroxidase. A cylindrical magnetic stirrer was specially designed to hold the immobilized enzymes firmly and to allow the reaction minzymic transformation quickly. Blood plasma can be assayed directly with no pretreatment. Ascrobic acid, uric acid, and creatinine in concenctrations of 0.25, 0.25, and 0.2 g/liter, respectively, did not interfere. The linearity of the assay was extended to 4.0 g of glucose concentrations. Results by our technique and by the otoluidine or hexokinase methods agreed well. The immobilized enzymes are stable for several months and can be used for several hundred highly accurate and reproducible assays.

Aspergillus niger↗
PubMed2000

Effects of chronic cold exposure on the activities of cytochrome c oxidase, glutathione peroxidase and glutathione reductase in rat tissues (Rattus norvegicus).

The effects of cold acclimation on the activity levels of cytochrome c oxidase, glutathione peroxidase and glutathione reductase in various tissues of the rat (Rattus norvegicus) were investigated. One group was individually housed at 4 +/- 1 degrees C and the other at 24 +/- 1 degrees C for 6 months. Chronic cold acclimation resulted in significantly (P < 0.05) increased cytochrome c oxidase activity levels in liver, kidney, heart, interscapular brown adipose tissue and gastrocnemius muscle. The activity of glutathione peroxidase was significantly (P < 0.05) elevated in liver, interscapular brown adipose tissue, lung and muscle, whereas glutathione reductase was only significantly (P < 0.05) elevated in interscapular brown adipose tissue as a result of chronic cold exposure. The results obtained are possibly indicative of a positive compensatory response against the increased production of oxygen derived radicals as a result of chronic cold exposure.

Acclimatization↗
PubMed2003

Determination of lactate or oxalate using injected lactate oxidase and peroxidase by capillary electrophoresis with UV detection.

Two reactions, catalyzed by lactate oxidase (LO) and peroxidase, are initiated by a single injection of the enzymes and the substrate 2,2'-azino-bis(3-ethylene-thiazoline-6-sulfonic acid) (ABTS) into the capillary previously filled with the sample (lactate or lactate-oxalate mixture) and the run buffer containing NADH. The oxidized ABTS product upon reaction with NADH is converted to NAD(+) which is separated and detected in less than 2 min at 266 nm with a sample throughput of 7 min (including wash steps between samples). Simplex trade mark software is used to optimize the enzyme concentrations and reaction temperature. Consumption of the more expensive LO enzyme is only 1.4 x 10(-3) U per assay assuming 27 nL per injection. Linearity is established within the range from 0.0025 to 1 mM with R(2) of 0.9982. Recoveries of lactate from five spiked serum samples averaged 101%. Application of this method for the determination of oxalate as an inhibitor of LO is demonstrated.

Electrophoresis, Capillary↗
PubMed2005

Determination of serum glucose using co-immobilized glucose oxidase and peroxidase onto arylamine glass beads affixed on a plastic strip.

Glucose oxidase (GOD) from Aspergillus niger and horseradish peroxidase (POD) were co-immobilized onto arylamine glass beads affixed on a plastic strip with a conjugation yield of 28.2 mg/g and 43% retention of their initial specific activity. The coimmobilized enzymes showed maximum activity at pH 7.5 when incubated at 37 degrees C for 15 min. A simple, specific and sensitive method for discrete analysis of the serum glucose was developed employing this strip. The minimum detection limit of the method was 5 mg/dl. Within and between assay coefficient of variations for the serum were <5.6% and <10.6% (n = 6) respondely. A good correlation (r = 0.943) was found between the glucose values obtained by the enzyme colorimetric method employing free GOD and POD and the present method. The strip lost 50% of its initial activity after its 150 regular uses for a period of one month, when stored in reaction buffer at 4 degrees C. The method is cost-effective than the enzymic colorimetric method, as the enzyme strip is reusable.

Adult↗