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PubMed1976

Mechanisms of electron transfer from sulfite to horseradish peroxidase-hydroperoxide compounds.

Using a rapid-scan spectrophotometer equipped with a stopped-flow apparatus, reactions of sulfite with compounds I and II of two horseradish peroxidase isoenzymes A and C were investigated. The direct two-electron reduction of peroxidase compound I by sulfite occurred at acidic pH but the mechanism gradually changed to the two-step reduction with the intermediate formation of compound II as the pH increased. The pH at which the one- and two-electron changes occurred at the same speed was 4.5 for peroxidase A and 7.7 for peroxidase C. A new peroxidase intermediate was found in the reaction between peroxidase compound II and sulfite. The sulfite compound showed a characteristic absorption band at 850 nm and the optical spectrum was similar to that of isoporphyrins but was quite different from that of sulfhemoproteins. The rate (k) of conversion from the sulfite-compound II complex to the sulfite compound was proportional to the concentration of H+ and the log k vs. pH plot for peroxidase A moved to the acidic side by 1.1 pH unit from that for peroxidase C.

Electron Transport↗
PubMed1997

Peroxidase substrates stimulate the oxidation of hydralazine to metabolites which cause single-strand breaks in DNA.

Hydrazines are believed to be oxidized by peroxidases to reactive intermediates responsible for a variety of adverse side effects including cancer and drug-induced lupus. However, hydrazines are regarded as a poor peroxidase substrates because inactivation of the peroxidase occurs during oxidation of these compounds. We have investigated the hypothesis that efficient peroxidase substrates, termed mediators, may stimulate peroxidase-catalyzed oxidation of hydrazines to intermediates capable of causing DNA damage. Oxidation of hydralazine by horseradish peroxidase was stimulated, enzyme inactivation was significantly decreased, and DNA strand breakage was enhanced by the addition of chlorpromazine. Similar results were obtained using other peroxidases, mediators, and hydrazine derivatives. DNA damage required the addition of a minimum of 3 equiv of hydrogen peroxide, suggesting the involvement of a three-electron oxidation product of hydralazine in DNA damage. Efficient substrates may therefore play a critical role in peroxidase-dependent oxidative metabolism and subsequent damage to biological macromolecules by certain chemicals.

DNA Damage↗
PubMed2001

Substrates and products of eosinophil peroxidase.

Eosinophil peroxidase has been implicated in promoting oxidative tissue damage in a variety of inflammatory conditions, including asthma. It uses H(2)O(2) to oxidize chloride, bromide and thiocyanate to their respective hypohalous acids. The aim of this study was to establish which oxidants eosinophil peroxidase produces under physiological conditions. By measuring rates of H(2)O(2) utilization by the enzyme at neutral pH, we determined the catalytic rate constants for bromide and thiocyanate as 248 and 223 s(-1) and the Michaelis constants as 0.5 and 0.15 mM respectively. On the basis of these values thiocyanate is preferred 2.8-fold over bromide as a substrate for eosinophil peroxidase. Eosinophil peroxidase catalysed substantive oxidation of chloride only below pH 6.5. We found that when eosinophil peroxidase or myeloperoxidase oxidized thiocyanate, another product besides hypothiocyanite was formed; it also converted methionine into methionine sulphoxide. During the oxidation of thiocyanate, the peroxidases were present as their compound II forms. Compound II did not form when GSH was included to scavenge hypothiocyanite. We propose that the unidentified oxidant was derived from a radical species produced by the one-electron oxidation of hypothiocyanite. We conclude that at plasma concentrations of bromide (20-120 microM) and thiocyanate (20-100 microM), hypobromous acid and oxidation products of thiocyanate are produced by eosinophil peroxidase. Hypochlorous acid is likely to be produced only when substrates preferred over chloride are depleted. Thiocyanate should be considered to augment peroxidase-mediated toxicity because these enzymes can convert relatively benign hypothiocyanite into a stronger oxidant.

Bromides↗
PubMed2001

The role of distal tryptophan in the bifunctional activity of catalase-peroxidases.

Catalase-peroxidases are bifunctional peroxidases exhibiting an overwhelming catalase activity and a substantial peroxidase activity. Here we present a kinetic study of the formation and reduction of the key intermediate compound I by probing the role of the conserved tryptophan at the distal haem cavity site. Two wild-type proteins and three mutants of Synechocystis catalase-peroxidase (W122A and W122F) and Escherichia coli catalase-peroxidase (W105F) have been investigated by steady-state and stopped-flow spectroscopy. W122F and W122A completely lost their catalase activity whereas in W105F the catalase activity was reduced by a factor of about 5000. However, the mutations did not influence both formation of compound I and its reduction by peroxidase substrates. It was demonstrated unequivocally that the rate of compound I reduction by pyrogallol or o-dianisidine sometimes even exceeded that of the wild-type enzyme. This study demonstrates that the indole ring of distal Trp in catalase-peroxidases is essential for the two-electron reduction of compound I by hydrogen peroxide but not for compound I formation or for peroxidase reactivity (i.e. the one-electron reduction of compound I).

Bacterial Proteins↗
PubMed1994

Vesicular transport of peroxidase in human eosinophilic myelocytes.

We performed ultrastructural cytochemistry to detect peroxidase in developmentally arrested human eosinophilic myelocytes. Human umbilical cord blood mononuclear cells were cultured for 21 days in the presence of murine-derived conditioned media, resulting in the development of eosinophilic myelocytes. Unlike normally developing eosinophilic myelocytes, which contain peroxidase in synthetic organelles (i.e. cisterns surrounding the nucleus and bounded by the rough endoplasmic reticulum and Golgi structures) and in immature and mature granules, the developmentally arrested cells showed ultrastructural evidence of decreased synthesis and secretory transport of peroxidase. Thus, peroxidase was generally absent in the perinuclear and rough endoplasmic cisterns, in Golgi structures, in immature granules and in the matrix compartment of most mature granules. Rather, biocompartmental specific granules displayed empty, peroxidase-negative matrix and central, peroxidase-negative core material. Peroxidase was present in perigranular vesicles, some of which were attached to granules. Such peroxidase-loaded transport vesicles are similar to those that effect piecemeal degranulation of mature human eosinophils cultured in rhIL-5-containing media [1]. These findings establish vesicle-mediated piecemeal degranulation in the secretory repertoire of immature human eosinophils and suggest the possibility that eosinophilic myelocytes may participate in vivo in important physiological and/or pathological events that require selective secretion from the specific granule matrix compartment.

Animals↗
PubMed1986

Activation of macrophages by peroxidases.

Peritoneal macrophages from C57BL/6 mice were activated in vitro with various peroxidases and their cytotoxic activity toward 3T12 cells was determined. Destruction of 3T12 cells by macrophages stimulated with horseradish peroxidase, lactoperoxidase, and microperoxidase was observed at peroxidase concentrations as low as 9, 1.6, and 200 nM, respectively. A 50% cytotoxic effect was obtained at peroxidase concentrations of 0.9, 1.6, and 1.5 microM, respectively. The macrophage-stimulating activity of horseradish peroxidase was not destroyed by boiling. This, together with the high activity of microperoxidase, indicates that the macrophage-stimulating activity of the peroxidases is probably associated with the heme portion of the enzymes. On a molar basis the peroxidases are much less potent macrophage activators than interferon (alpha + beta) and endotoxin. Nevertheless, our data clearly indicate that peroxidases are a group of enzymes capable of inducing macrophage activation, resulting in cytostatic and/or cytocidal activity.

Animals↗
PubMed1985

Structure of an electron transfer complex. II. Chemical modification of carboxyl groups of cytochrome c peroxidase in presence and absence of cytochrome c.

Cytochrome c peroxidase forms an electron transfer complex with cytochrome c. The complex is governed by ionic bonds between side chain amino groups of cytochrome c and carboxyl groups of peroxidase. To localize the binding site for cytochrome c on the peroxidase, we have used the method of differential chemical modification. By this method the chemical reactivity of carboxyl groups (toward carbodiimide/aminoethane sulfonate) was compared in free and in complexed peroxidase. When ferricytochrome c was bound to cytochrome c peroxidase, acidic residues 33, 34, 35, 37, 221, 224, and 1 to 3 carboxyls at the C terminus became less reactive by a factor of approximately 4, relative to the remaining 39 carboxylates of peroxidase. Of the less reactive residues those in the 30-40 region and the 221/224 pair are on opposite sides of the surface area which contains the heme propionates. We, therefore, propose that the binding site for cytochrome c on cytochrome c peroxidase spans the area where one heme edge comes close to the molecular surface. The results are in very good agreement with chemical cross-linking studies (Waldmeyer, B., and Bosshard, H.R. (1985) J. Biol. Chem. 260, 5184-5190); they also support a hypothetical model predicted on the basis of the known crystal structures of cytochrome c and peroxidase (Poulos, T.L., and Kraut, J. (1980) J. Biol. Chem. 255, 10322-10330).

Binding Sites↗
PubMed1987

The mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen peroxide.

Formation of oxyperoxidase from the reaction of ferryl horseradish peroxidase with H2O2 is inhibited by a small amount of tetranitromethane (TNM), a powerful scavenger of superoxide anion radical. The inhibition by TNM, however, does not exceed 35% as the TNM concentration is increased above 5 microM. The stoichiometry of the reaction in the presence of TNM suggests the following equation for TNM-sensitive formation of oxyperoxidase. Ferryl peroxidase + H2O2----(ferric peroxidase + O2- + H+)----oxyperoxidase The kinetic study on the TNM-resistant formation of oxyperoxidase suggests that the displacement of the oxygen with H2O2 takes place at the sixth coordination position at maximal rates of 0.048 and 0.054 s-1 for peroxidases A and C, respectively, at 5 degrees C. The TNM-sensitive and -resistant reactions are concluded to occur in parallel, and both yield oxyperoxidase. In either mechanism, the protonated form of ferryl peroxidase is active and the pK alpha value is 7.1 for peroxidase A and 8.6 for peroxidase C. Oxyperoxidase decomposes spontaneously with a large activation energy (23.0 kcal/mol), and the reaction of ferryl peroxidase with H2O2 reaches a steady level of oxyperoxidase, which depends on pH and the concentration of H2O2.

Ferric Compounds↗
PubMed1978

An analysis on the specificity of the histochemical techniques already proposed to detect catalases and peroxidases.

The spot test carried on filter paper strips appears as a very suitable technique to investigate the reactivity of catalases, peroxidases, porphyrins (bilirubin and protoporphyrin), metalloporphyrins (haemoglobin, haemin, haematin, chlorophyll and cyanocobalamin), ferric and ferrous salts. By using this technique the specificity of the already proposed techniques admitted as appropriate to detect histochemically peroxidases and catalases was investigated. The results shown from the already proposed techniques to detect peroxidases only the alpha-naphthol reaction is somewhat specific for this enzyme, if the results were taken immediately. However, if the results were taken after 24 h, the reaction loose all specificity. The other techniques proposed to detect peroxidase are not specific, either concerning the discrimination between catalases and peroxidases activity or regarding the possibility to differenciate an enzymic from a catalytic activity provided by haemic iron containing compounds and sometimes by iron salts. Our histochemical technique already proposed as suitable to detect catalases seams to be specific, since peroxidases do not react positively. By replacing benzidine for some others hydrogen donors the peroxidases histochemical techniques remain not specific and are unable to discriminate this enzyme from catalases. Porphyrins (protoporphyrin and bilirubin), magnesium and cobalt containing metalloporhyrins (chlorophyll and cyanocobalamin) do not produce oxidation of any hydrogen donors used. Iron salts are also able to give positive results with some techniques already proposed as suitable for peroxidases and catalases detection.

Animals↗
PubMed1998

Effect of pH on tobacco anionic peroxidase stability and its interaction with hydrogen peroxide.

The effect of extremely acidic pH on the stability of tobacco peroxidase and lignin peroxidase holoenzymes has been studied. Stabilization of tobacco peroxidase holoenzyme in the presence of calcium cations at pH < 2 and stabilization of lignin peroxidase at pH > 2 in the presence of veratryl alcohol have been shown. The dependence of the reaction rate constant for hydrogen peroxide interaction with tobacco peroxidase on pH suggests that the reaction rate is under control of a group with pK of 2.5. A tobacco peroxidase model structure has been created by means of homology modeling on the basis of the tobacco peroxidase sequence and the coordinates of peanut peroxidase crystal structure. The model structure demonstrates the presence of the negatively charged Glu-141 at the entrance to the active site and its electrostatic repulsion from heme propionates and triad of Asp-76, -79, and -80 residues. The results on tobacco holoperoxidase stabilization at pH 1.8 in the presence of calcium cations and drop in reaction rate constant for the enzyme interaction with hydrogen peroxide are explained by a hypothetical formation of ionic bonds between Glu-141 and the triad of aspartic acid residues via calcium cation lowering the accessibility of the active site and stabilizing the holoenzyme.

Amino Acid Sequence↗
PubMed1996

Mechanism of simultaneous iodination and coupling catalyzed by thyroid peroxidase.

Thyroid peroxidase (TPO) simultaneously catalyzes two very different types of reaction in the thyroid gland- iodination and coupling. The present study addresses the mechanism of this simultaneous dual activity. Compound I, the two-electron oxidation product of TPO, exists in two different forms--an oxoferryl porphyrin pi-cation radical and an oxoferryl protein radical. It has been proposed that iodination is mediated by the porphyrin pi-cation radical form of TPO compound I, while coupling is mediated by the protein radical form. However, results obtained in the present study favor the view that both iodination and coupling are mediated by the porphyrin pi-cation radical form of compound I. In the first part of the study, we compared coupling and iodination activities of two peroxidases with very similar crystal structures--cytochrome c peroxidase (CcP) and lignin peroxidase (LiP). Although these two peroxidases have very similar three-dimensional structures, CcP forms a compound I only of the protein radical type, whereas compound I of LiP exists only as a porphyrin pi-cation radical. Comparison of the catalytic activities of the two enzymes showed that diiodotyrosine (DIT)-stimulated coupling activity of LiP was significantly greater than that of CcP. Moreover, lignin peroxidase displayed very significant iodinating activity at acid pHs, whereas iodination with CcP was negligible at all pHs tested. Our findings with these two structurally similar peroxidases suggested that TPO-catalyzed iodination and coupling could both be mediated by the porphyrin pi-cation radical form of compound I. More direct evidence in support of this view was obtained in the second part of this study, employing TPO and lactoperoxidase (LPO) model systems in which iodination and coupling occurred simultaneously. Heme spectral analysis was used to correlate formation of the protein radical form of compound I with the kinetics of the iodination and coupling reactions. Formation of the compound I protein radical was not observed until the iodination and coupling reactions had almost been completed. In separate experiments it was shown that the spontaneous conversion of the porphyrin pi-cation radical form of TPO or LPO compound I to the protein radical form was markedly inhibited by a low concentration of iodide, especially in the presence of an iodide acceptor. These studies provide compelling evidence that both iodination and coupling are mediated by the porphyrin pi-cation radical form of compound I. This was further substantiated by the finding that coupling was inhibited in the presence of excess iodide, an observation readily explained by competition between iodide and DIT residues in thyroglobulin for oxidation by the porphyrin pi-cation radical.

Animals↗
PubMed1991

Tissue peroxidase in the normal and neoplastic salivary gland.

Peroxidase activity was measured by two colorimetric methods in six neoplastic tumors of the parotid salivary gland. When p-phenylenediamine was used as the hydrogen donor co-substrate, peroxidase activity was absent or reduced from 6 to 22% of normal in these tumors. Cross reactivity with normal peroxidase antibody could not be demonstrated in tumors exhibiting negative activity. Two neoplastic salivary glands had well-described, encapsulated tumors which showed reduced peroxidase activity when compared with the normal uninvolved portion. However, when guaiacol was substituted for p-phenylenediamine, normal activity was recorded. After dialysis, peroxidase activity was not enhanced. Mixing experiments showed no effect of the tumor extract on the peroxidase activity of normal saliva, nor on salivary gland supernatant. Normal salivary gland peroxidase was inhibited 90% by 10(-2) g/L amino-triazole, but neoplastic tumors were inhibited less (13 and 73%). It is suggested that peroxidase is a simple marker for the detection of neoplasia and can be of value in the differentiation of benign tumors.

Adenoma↗
PubMedDate not supplied

Metal ions-dependent peroxidase and oxidoreductase activities of polyclonal IgGs from the sera of Wistar rats.

We present evidence showing that a small fraction of electrophoretically homogeneous IgGs from the sera of healthy Wistar rats is bound with several different Me2+ ions and oxidizes 3,3'-diaminobenzidine through a peroxidase activity in the presence of H2O2 and through an oxidoreductase activity in the absence of H2O2. During purification on Protein A-Sepharose and gel filtration, the polyclonal IgGs partially lose the Me2+ ions. Therefore, in the absence of external metal ions, the specific peroxidase activity of IgGs from the sera of different rats varied in the range 1.6-26% and increased up to 13-198% after addition of Fe2+ or Cu2+ ions as compared with horseradish peroxidase (HRP, taken for 100%). The oxidoreductase activity of HRP is 24-fold lower than its peroxidase activity, while oxidoreductase and peroxidase activities of IgGs are comparable. Oxidoreductase activities of different IgGs in the absence of external metal ions varied from 22 to 800%, and in the presence of Fe2+ or Cu2+ ions, from 37 to 1100% in comparison with the HRP oxidoreductase activity (100%). Chromatography of the IgGs on Chelex-100 leads to the adsorption of a small IgG fraction bound with metal ions and to its separation to many different subfractions demonstrating various affinities to the chelating resin and increased levels of the specific oxidoreductase and peroxidase activities. Antioxidant enzymes such as superoxide dismutases, catalases, and glutathione peroxidases are known to represent critical defense mechanisms for preventing oxidative modifications of DNA, proteins, and lipids. Peroxidase and oxidoreductase activity of antibodies may play an important role in the protection of organisms from oxidative stress and toxic compounds.

Animals↗
PubMed1991

Ontogeny of peroxidase activity in epithelium and eosinophils of the mouse uterus.

Outbred CD-1 mice treated for 1 or 4 days with 1 mg/kg of diethylstilbestrol (DES) at various ages after birth were examined for histochemical localization of peroxidase in the uterine epithelium. Peroxidase activity in uterine extracts was also measured by a radiometric assay and the conversion of [3H]DES to [3H]Z,Z-diensestrol (Z,Z-DIES). While no peroxidase activity was detected by a histochemical method in uterine epithelium from untreated 5-day old mice, the enzyme was apparent in mice treated for 4 days with DES; uterine eosinophils were absent at this age. By day 9, DES-induced staining for peroxidase in uterine epithelial cells and the number of uterine eosinophils had increased significantly. In addition, at this age, the biochemical assays for uterine peroxidase were sensitive enough to show that DES is converted to Z,Z-DIES and that [3H]estradiol gives rise to 3H2O and water-soluble radioactive metabolites. The peroxidase response to DES, determined by both histochemical and biochemical methods, increased with the age of the immature mice. These data indicate that the neonatal uterus, although deficient in eosinophils, demonstrates a peroxidase response to estrogen and that this response is localized primarily in the luminal epithelium. The role of this DES-induced peroxidase activity in converting DES to activated metabolites that may cause cell damage is discussed.

Age Factors↗
PubMed1995

Heterologous expression of selenium-dependent glutathione peroxidase affords cellular resistance to paraquat.

Transfection of murine NIH3T3 fibroblasts and human MCF7 breast carcinoma cells with a pSV2-derived eukaryotic expression vector for human cytosolic glutathione peroxidase resulted in clones with increased glutathione peroxidase activity. This heterologous expression indicates that murine cells recognize the human "selenocysteine insertion sequence" in the 3' untranslated region of the mRNA which facilitates insertion of selenocysteine directed by the opal codon. Though most clones from both cell lines eventually lost their enhanced glutathione peroxidase activity despite continuous selection on G418, some NIH3T3 clones retained enhanced enzyme activity without continuous G418 exposure. Transfection of MCF7 cells with an Epstein-Barr virus (EBV)-derived episomally replicating expression vector carrying the glutathione peroxidase gene also revealed increased glutathione peroxidase activity. These MCF7 cells, however, all required exposure to G418 to maintain enhanced glutathione peroxidase activity. Detailed biochemical analysis of a stably expressing NIH3T3 clone and MCF7 expressing cells revealed no alterations in activities of copper-zinc superoxide dismutase, manganese superoxide dismutase, catalase, phospholipid-glutathione peroxidase, glutathione reductase, glutathione transferase, or NADPH-P450 reductase. Both pSV2- and EBV-derived glutathione peroxidase-expressing clones exhibited enhanced resistance to paraquat as well as to peroxides.

3T3 Cells↗
PubMed1996

The effect of veratryl alcohol on manganese oxidation by lignin peroxidase.

The extracellular peroxidase isozymes secreted by the white rot fungus Phanerochaete chrysosporium have been classified as manganese peroxidases (isozymes H3, H4, H5, and H9) and lignin peroxidases (isozymes H1, H2, H6, H7, H8, and H10). Recently we reported peroxidase isozyme H2 can also oxidize Mn2+ (Khindaria et al., 1995, Biochemistry 34, 7773-7779). This lignin peroxidase isozyme oxidized Mn2+ with both of the enzyme intermediates, compound I and compound II, at the same rates as manganese peroxidase isozyme H4. The results of single-turnover kinetic studies have now demonstrated that compound I of the other lignin peroxidase isozymes (H1, H6, H7, H8, and H1O) also readily oxidized Mn2+, but that the rate of Mn2+ oxidation by compound II was extremely slow. Compound III rapidly the presence of Mn2+, oxalate, and H2O2. However, upon the addition of veratryl alcohol, the results indicated that veratryl alcohol served to reduce compound II. Under such conditions, compound III did not accumulate, and a steady-state rate of Mn2+ oxidation was observed. The rate of Mn2+ oxidation was the same as for the reduction of compound II by veratryl alcohol. The dependence of the rate of Mn2+ oxidation on the concentration of veratryl alcohol was consistent with a mechanism in which Mn2+ is oxidized by compound I and veratryl oxidized by compound II. Therefore, under physiologically relevant conditions, in which both veratryl alcohol and Mn2+ are present, all lignin peroxidase isozymes would be capable of oxidizing Mn2+ to Mn3+ which can serve as a diffusible oxidant.

Agaricales↗
PubMed1996

Phytohormone control of the tobacco anionic peroxidase promoter.

The tobacco anionic peroxidase gene encodes the predominant peroxidase isoenzyme in the aerial portions of tobacco. Three kb of the peroxidase promoter was joined to the coding region of the Escherichia coli beta-glucuronidase gene (GUS), and transiently expressed in tobacco mesophyll protoplasts in the presence or absence of plant growth regulators. Benzyladenine, ethylene, and gibberellic acid did not affect peroxidase gene expression. Abscisic acid slightly inhibited expression at high concentrations. The auxins indole-3-acetic acid (IAA) and naphthaleneacetic acid strongly suppressed peroxidase expression. We observed half maximal suppression at 30 microM IAA. An anti-auxin, p-chlorophenoxyisobutyric acid (PCIB), enhanced expression from the peroxidase promoter above that of untreated controls or restored activity when used in combination with IAA. Sequencing 3 kb of the peroxidase promoter revealed many potential regulatory elements based on sequence homology to previously characterized genes. This includes several consensus transcription factor binding sites found in auxin-regulated promoters. 5' deletions of the peroxidase promoter/GUS fusion revealed several positive and negative regulatory elements. An upstream enhancer element was found between -3146 and -638 from the start of transcription. A strong silencer element was observed between -638 and -220. Removal of this silencer resulted in a truncated promoter (-220) with 100% activity of the full-length promoter (-3146). Inhibition by auxin was observed with all 5' deletions.

Base Sequence↗
PubMed1981

Heat-stability of peroxidase in mycelia of some toxigenic and nontoxigenic aspergilli and penicillia.

Seven-day-old mycelia from 19 cultures of Aspergillus and 12 cultures of Penicillium were heated to 50, 60, 65, 70, 75, 80, 85, 90 or 95 C for no more than 1 min, and tested for residual peroxidase. The peroxidase from all aspergilli survived heating at 50 through 80 C. Peroxidase from toxigenic strains of Aspergillus flavus, Aspergillus parasiticus and Aspergillus ochraceus survived heating at 85 C and often at 90 C, whereas peroxidase from non-toxigenic strains of A. flavus was inactivated at 90 C and markedly reduced in activity at 85 C. Peroxidase from all penicillia survived heating at all temperatures through 80 C, although the activity of several cultures was reduced at 80 C. Peroxidase activity in mycelia of two strains of Penicillium cyclopium and one of Penicillium puberulum failed to survive heating at 85 C. One strain each of Penicillium roqueforti and Penicillium viridicatum exhibited some peroxidase activity after heating at 90 C, whereas the peroxidase of all other penicillia was inactivated at this temperature.

Aflatoxins↗