In vitro degradation of aflatoxin B1 by horse radish peroxidase

Das, Chitrangada; Mishra, Hari Niwas

doi:10.1016/s0308-8146(99)00196-x

Cited by 32 publications

(17 citation statements)

References 13 publications

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“…Doyle and Marth studied the degradation of AFs by lactoperoxidase at 5, 50 and 500 U mL −1 in a reaction medium containing 225 µmol L −1 NaCl and 50 µmol L −1 H 2 O 2 at 28 °C for 24 h and demonstrated that the degradation rate increased from 3.6% to 5.1% and from 4.6% to 7.2% for AFB 1 and AFG 1 , respectively, when the amount of enzyme was increased from 50 to 500 U mL −1 . The enzymatic biodegradation of AFB 1 was also proposed by Das and Mishra, where different POD concentrations (between 2 and 16 U) evaluated in the degradation of AFB 1 (3.2 µg) resulted in a marked increase in the reaction rate in the experiments using from 2 to 8 U, but above 10 U, the degradation percentage reached a stable level (60%). Therefore, the present study demonstrates a high biotransformation using low enzyme concentration when compared with other studies.…”

Section: Resultsmentioning

confidence: 62%

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Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Sibaja

Garcia

Feltrin

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND Aflatoxin B1 (AFB1) is the most commonly occurring and the most toxic of all aflatoxins (AFs). It is responsible for liver cancer in animals and it is listed as a Group I carcinogen by the International Agency for Research on Cancer. Thus, it is necessary to find decontamination methods that show efficiency, specificity, low cost, and that allow the disposal of contaminated raw materials into the environment. This study evaluated the effects of enzyme concentration, pH, temperature and reaction time on AFB1 biotransformation by commercial peroxidase (POD) in a model solution (100 mmol L−1 phosphate buffer). RESULTS When 0.015 U mL−1 was used to treat 0.5 µg L−1 of AFB1, at pH 7.0–8.0 and 30–40 °C, for 8.0 h, the AFB1 biotransformation reached its maximum (97%). KM value of POD for the biotransformation of AFB1 was 0.0160 µmol L−1 (5 µg L−1) with a VMAX of 6.4 µmol L−1 min−1, which were determined based on Lineweaver‐Burk's plot. POD (0.015 U mL−1) effectively reduces AFB1 (97%) and M1 (65%) in UHT milk and AFB1 (24%) in lager beer samples acquired in markets of Rio Grande‐RS (Brazil). CONCLUSION The use of POD may be a strategy to mitigate the impact of AFs found in food to reduce the risk of consumer exposure. © 2018 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 62%

“…The use of enzymes, including oxidases, reductases, laccases, and peroxidases (PODs), has proven to effectively degrade AFs in aqueous medium. However, the mechanism of enzyme‐catalyzed AF degradation and the kinetics of the reaction between commercial PODs and AFs remain unknown.…”

Section: Introductionmentioning

confidence: 99%

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Sibaja

Garcia

Feltrin

et al. 2018

J of Chemical Tech & Biotech

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“…incubation time at atmospheric pressure. Hydrogen peroxide was used in a concentration of 5 mM (Das and Mishra 2000). The DMSO extract of reaction mixture after detoxification was designated as solution B.…”

Section: Detoxification Of Groundnut Meal Infected With Aflatoxinmentioning

confidence: 99%

Effect of detoxified Aflatoxin B1 contaminated products on some in vivo and in vitro plant physiological systems

Das

Mishra

2001

Acta Physiol Plant

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Aflatoxin BI was detoxified (60 %) enzymatically by horseradish peroxidase. In another set of experiments the toxin was detoxified (97 %) by a combination of enzyme and microwave treatments. Chloroform extracts of these reaction products were used to study their effects on some important physiological processes of higher plants. Cell mass growth in suspension culture of Catharanthus roseus showed 34 % and 77 % respective increase in dry weight after 4 to 8 weeks of incubation at room temperature (22 EC) without toxin but in presence of toxin only 21% and 43 % dry weight increase occurred in the same time interval. Aflatoxin B 1 showed a profound effect on pollen germination and pollen tube morphology leading to only 40 % germination and several morphological anomalies in Catharanthus roseus and Haemanthus Katherinae. Embryogenic callus of Santalum album could give rise to only 60 % somatic embryo in presence of lmM toxin with several abnormalities which is much less compared to 94 % conversion to distinct bipolar embryos in case of control set without toxin. Only 49 % seeds ofArachis hypogaea germinated in presence of 1 mM aflatoxin in the germinating medium compared to 71 % germination in control media.

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“…Peroxidase (POD), of which active cite is Fe-protoporphyrin, was reported to catalyze oxidative reactions of a wide range of mutagens and carcinogens including HCAs, thereby decreasing the mutagenicity and carcinogenicity. 5,6) In the above cases, metal-porphyrin derivatives serve as an adsorbent of HCAs or a catalysis of oxidative reaction of mutagens.On the other hand, we previously reported that some anion-exchangers modified with metal-tetrakis(sulfophenyl)-porphines (M-TSPP r ) exhibited a peroxidase (POD)-like activity and was applicable to the determination of hydrogen peroxide as a solid-mimesis of horse radish POD. 7,8) In the present paper, we investigated the POD-like activity of M-TSPP r s in the oxidation of HCAs to elucidate the usefulness of M-TSPP r s as a POD-like catalyst in the oxidation of HCAs.…”

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confidence: 99%

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confidence: 99%

Peroxidase-Like Catalytic Activity of Anion-Exchange Resins Modified with Metal-Porphyrins in Oxidative Reaction of Hetrocyclic Amines with Hydrogen Peroxide

Mifune

Hino

Sugita

et al. 2005

CHEMICAL & PHARMACEUTICAL BULLETIN

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Heterocyclic amines (HCAs, Fig. 1) are mutagenic factors that are predominantly ingested as pyrolysis products of meats and fishes.1) To adsorb the HCAs on ligands, a cellulose coupled with a Cu-phthalocyanine derivative (Cu-PC, a related compound metal-porphyrin), so-called "blue cotton," was developed, 2,3) which was reported to be beneficial for callbacks and determinations of HCAs in environmental waters 2) and air-born particules.4) The adsorption of HCAs on the blue cotton is caused by hydrophobic p-p interaction between HCAs and Cu-PC coupled with cotton fiber. Peroxidase (POD), of which active cite is Fe-protoporphyrin, was reported to catalyze oxidative reactions of a wide range of mutagens and carcinogens including HCAs, thereby decreasing the mutagenicity and carcinogenicity. 5,6) In the above cases, metal-porphyrin derivatives serve as an adsorbent of HCAs or a catalysis of oxidative reaction of mutagens.On the other hand, we previously reported that some anion-exchangers modified with metal-tetrakis(sulfophenyl)-porphines (M-TSPP r ) exhibited a peroxidase (POD)-like activity and was applicable to the determination of hydrogen peroxide as a solid-mimesis of horse radish POD. 7,8) In the present paper, we investigated the POD-like activity of M-TSPP r s in the oxidation of HCAs to elucidate the usefulness of M-TSPP r s as a POD-like catalyst in the oxidation of HCAs. We revealed that some M-TSPP r s exhibit a similar POD-like activity for HCAs to horse radish POD. In particular, Fe-and Mn-TSPP r s catalyze the oxidation of 2-amino-3-methyl-imidazo[4,5-f ]quinoline (IQ) with hydrogen peroxide. The resulting IQ-dimmer has no mutagenicity in umutest. We elucidated that M-TSPP r can decrease mutagenicity of HCAs in vitro through its POD-like catalytic activity. ExperimentalMaterials Tetrakis(sulfophenyl)porphine (H 2 -TSPP) was purchased from Wako Junyaku Co. Ltd. (Osaka, Japan). Mutagenic HCAs (see Fig. 1), IQ, MeIQ, MeIQx, TrpP-1 and TrpP-2, were purchased from Wako Junyaku Co. Ltd. GluP-1 and GluP-2 (Chemsyn Science Laboratories, Lenaxa, Kansas, U.S.A.) were kindly donated from Prof. Hikoya Hayatsu (Shujitsu University). They were used without further purification. An anion-exchange resin, Amberlite IRA 900 (24-42 mesh) in nitrate form, was a manufacture of Organo Chemical Co. Ltd. (Tokyo, Japan). Other reagents were of analytical or reagent grade. umu-Test kit was purchased from Japan Immunoresearch Laboratories Co. Ltd. (Takasaki, Japan).Apparatus Absorption (UV/V) spectra and absorbances (abbr. "A") were measured on a Shimadzu UV-180 or a JASCO V-570 spectrophotometer with 10 mm quartz cells. HPLC system was constructed with a Shimadzu pump (LC-6A), a Shimadzu photodiode array detector (SPD-M6A) and a To elucidate the peroxidase (POD)-like catalytic activity of anion-exchange resins modified with metaltetrakis(sulfophenyl)porphine (M-TSPP r s), an oxidative reaction of seven mutagenic heterocyclic amines (HCAs) with hydrogen peroxide, which reaction is catalyzed by horse radish POD, was investigate...

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In vitro degradation of aflatoxin B1 by horse radish peroxidase

Cited by 32 publications

References 13 publications

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Effect of detoxified Aflatoxin B1 contaminated products on some in vivo and in vitro plant physiological systems

Peroxidase-Like Catalytic Activity of Anion-Exchange Resins Modified with Metal-Porphyrins in Oxidative Reaction of Hetrocyclic Amines with Hydrogen Peroxide

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