Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
권호 표지
DOI QR코드

DOI QR Code

Detoxification of Aflatoxin B1 Contaminated Maize Using Human CYP3A4

  • Yamada, Marie (Division of Signal Responses, Biosignal Research Center, Kobe University) ;
  • Hatsuta, Koji (Division of Signal Responses, Biosignal Research Center, Kobe University) ;
  • Niikawa, Mayuko (Division of Signal Responses, Biosignal Research Center, Kobe University) ;
  • Imaishi, Hiromasa (Division of Signal Responses, Biosignal Research Center, Kobe University)
  • Received : 2020.03.18
  • Accepted : 2020.05.11
  • Published : 2020.08.28
Download PDF
⟨ Previous Next ⟩

Abstract

Aflatoxin B1 (AFB1) is a mycotoxin produced by Aspergillus flavus (A. flavus). AFB1 is reported to have high thermal stability and is not decomposed by heat treatment during food processing. Therefore, in this study, knowing that AFB1 is metabolized by cytochrome P450 (CYP), our aim was to develop a method to detoxify A. flavus-contaminated maize, under normal temperature and pressure, using Escherichia coli expressing human CYP3A4. First, the metabolic activity of AFB1 by recombinant human CYP3A4 was evaluated. As a result, we confirmed that recombinant human CYP3A4 metabolizes 98% of AFB1. Next, we found that aflatoxin Q1, a metabolite of AFB1 was no longer mutagenic. Furthermore, we revealed that about 50% of the AFB1 metabolic activity can be maintained for 3 months when E. coli expressing human CYP3A4 is freeze-dried in the presence of trehalose. Finally, we found that 80% of AFB1 in A. flavus-contaminated maize was metabolized by E. coli expressing human CYP3A4 in the presence of surfactant triton X-405 at a final concentration of 10% (v/v). From these results, we conclude that AFB1 in A. flavus-contaminated maize can be detoxified under normal temperature and pressure by using E. coli expressing human CYP3A4.

Keywords

References

  1. Benkerroum N. 2019. Retrospective and prospective look at aflatoxin research and development from a practical standpoint. Int. J. Environ. Res. Public Health. 16: 3633. https://doi.org/10.3390/ijerph16193633
  2. Spanjer MC, Rensen PM, Scholten JM. 2008. LC-MS/MS multi-method for mycotoxins after single extraction, with validation data for peanut, pistachio, wheat, maize, cornflakes, raisins and figs. Food Addit. Contam. Part A Chem. Anal. Control Expo. Risk Assess. 25: 472-489. https://doi.org/10.1080/02652030701552964
  3. Spencer Smith J, Paul Williams W, Windham GL. 2019. Aflatoxin in maize: a review of the early literature from "moldy-corn toxicosis" to the genetics of aflatoxin accumulation resistance. Mycotoxin Res. 35: 111-128. https://doi.org/10.1007/s12550-018-00340-w
  4. Norlia M, Nor-Khaizura MAR, Selamat J, Abu Bakar F, Radu S, Chin CK. 2018. Evaluation of aflatoxin and Aspergillus sp. contamination in raw peanuts and peanut-based products along this supply chain in Malaysia. Food Addit. Contam. Part A Chem. Anal. Control Expo. Risk Assess. 35: 1787-1802. https://doi.org/10.1080/19440049.2018.1488276
  5. Raters M, Matissek R. 2008. Thermal stability of aflatoxin B1 and ochratoxin A. Mycotoxin Res. 24: 130-134. https://doi.org/10.1007/BF03032339
  6. Luo X, Wang R, Wang L, Li Y, Wang Y, Chen Z. 2014. Detoxification of aflatoxin in corn flour by ozone. J. Sci. Food Agric. 94: 2253-2258. https://doi.org/10.1002/jsfa.6550
  7. Womack ED, Brown AE, Sparks DL. 2014. A recent review of non-biological remediation of aflatoxin-contaminated crops. J. Sci. Food Agric. 94: 1706-1714. https://doi.org/10.1002/jsfa.6520
  8. Wild CP, Turner PC. 2002. The toxicology of aflatoxins as a basis for public health decisions. Mutagenesis 17: 471-481. https://doi.org/10.1093/mutage/17.6.471
  9. Imaishi H, Goto T. 2018. Effect of genetic polymorphism of human CYP2B6 on the metabolic activation of chlorpyrifos. Pestic. Biochem. Physiol. 144: 42-48. https://doi.org/10.1016/j.pestbp.2017.11.003
  10. Pelkonen O, Turpeinen M, Hakkola J, Honkakoski P, Hukkanen J, Raunio H. 2008. Inhibition and induction of human cytochrome P450 enzymes: current status. Arch. Toxicol. 82: 667-715. https://doi.org/10.1007/s00204-008-0332-8
  11. Tornio A, Backman JT. 2018. Cytochrome P450 in pharmacogenetics: an update. Adv. Pharmacol. 83: 3-32. https://doi.org/10.1016/bs.apha.2018.04.007
  12. Evans WE, Relling MV. 1999. Pharmacogenomics: translating functional genomics into rational therapeutics. Science 286: 487-491. https://doi.org/10.1126/science.286.5439.487
  13. Werk AN, Cascorbi I. 2014. Functional gene variants of CYP3A4. Clin. Pharmacol. Ther. 96: 340-348. https://doi.org/10.1038/clpt.2014.129
  14. Zanger UM, Schwab M. 2013. Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol. Ther. 138: 103-141. https://doi.org/10.1016/j.pharmthera.2012.12.007
  15. Wang H, Dick R, Yin H, Licad-Coles E, Kroetz DL, Szklarz G, et al. 1998. Structure-function relationships of human liver cytochromes P450 3A: aflatoxin B1 metabolism as a probe. Biochemistry 37: 12536-12545. https://doi.org/10.1021/bi980895g
  16. Kamdem LK, Meineke I, Godtel-Armbrust U, Brockmoller J, Wojnowski L. 2006. Dominant contribution of P450 3A4 to the hepatic carcinogenic activation of aflatoxin B1. Chem. Res. Toxicol. 19: 577-586. https://doi.org/10.1021/tx050358e
  17. Yamamoto R, Muroi K, Imaishi H. 2018. Serum derived from ulcerative colitis mouse changes the metabolism of the fluorescent substrate by P450 depending on the degree of disease progression. Chem. Biol. Interact. 290: 88-98. https://doi.org/10.1016/j.cbi.2018.05.012
  18. Imaishi H, Petkova-Andonova M. 2007. Molecular cloning of CYP76B9, a cytochrome P450 from Petunia hybrida, catalyzing the omega-hydroxylation of capric acid and lauric acid. Biosci. Biotechnol. Biochem. 71: 104-113. https://doi.org/10.1271/bbb.60396
  19. Hamer B, Bihari N, Reifferscheid G, Zahn RK, Muller WE, Batel R. 2000. Evaluation of the SOS/umu-test post-treatment assay for the detection of genotoxic activities of pure compounds and complex environmental mixtures. Mutat. Res. 466: 161-171. https://doi.org/10.1016/S1383-5718(00)00016-4
  20. Wang P, Chang PK, Kong Q, Shan S, Wei Q. 2019. Comparison of aflatoxin production of Aspergillus flavus at different temperatures and media: Proteome analysis based on TMT. Int. J. Food Microbiol. 310: 108313. https://doi.org/10.1016/j.ijfoodmicro.2019.108313
  21. Walton M, Egner P, Scholl PF, Walker J, Kensler TW, Groopman JD. 2001. Liquid chromatography electrospray-mass spectrometry of urinary aflatoxin biomarkers: characterization and application to dosimetry and chemoprevention in rats. Chem. Res. Toxicol. 14: 919-926. https://doi.org/10.1021/tx010063a
  22. Johnson WW, Guengerich FP. 1997. Reaction of aflatoxin B1 exo-8,9-epoxide with DNA: kinetic analysis of covalent binding and DNA-induced hydrolysis. Proc. Natl. Acad. Sci. USA 94: 6121-6125. https://doi.org/10.1073/pnas.94.12.6121
  23. Kamdem L, Meineke I, Godtel-Armbrust U, Brockmoller J, Wojnowski L. 2006. Dominant contribution of P450 3A4 to the hepatic carcinogenic activation of aflatoxin B-1. Chem. Res. Toxicol. 19: 577-586. https://doi.org/10.1021/tx050358e
  24. Guimaraes D, Noro J, Silva C, Cavaco-Paulo A, Nogueira E. 2019. Protective effect of Saccharides on freeze-dried liposomes encapsulating drugs. Front. Bioeng. Biotechnol. 7: 424. https://doi.org/10.3389/fbioe.2019.00424
  25. Prestrelski SJ, Tedeschi N, Arakawa T, Carpenter JF. 1993. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 65: 661-671. https://doi.org/10.1016/S0006-3495(93)81120-2
  26. Leslie S, Israeli E, Lighthart B, Crowe J, Crowe L. 1995. T Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying. Appl. Environ. Microbiol. 61: 3592-3597. https://doi.org/10.1128/AEM.61.10.3592-3597.1995
  27. Kankaapaa P, Tuomola E, El-Nezami H, Ahokas J, Salminen S. 2000. Binding of aflatoxin B-1 alters the adhesion properties of Lactobacillus rhamnosus strain GG in a Caco-2 model. J. Food Prot. 63: 412-414. https://doi.org/10.4315/0362-028X-63.3.412
  28. Schnaitman C. 1971. Effect of Ethylenediaminetetraacetic acid, triton X-100, and lysozyme on the morphology and chemical composition of isolated cell walls of Escherichia coli. J. Bacteriol. 108: 553-563. https://doi.org/10.1128/JB.108.1.553-563.1971
  29. Chen G, Wang M, Tian X, Wu Z. 2018. Analyses of Monascus pigment secretion and cellular morphology in non-ionic surfactant micelle aqueous solution. Microb. Biotechnol. 11: 409-419. https://doi.org/10.1111/1751-7915.13038

Cited by

  1. A Portable, Cost-Effective and User-Friendly Instrument for Colorimetric Enzyme-Linked Immunosorbent Assay and Rapid Detection of Aflatoxin B1 vol.10, pp.10, 2020, https://doi.org/10.3390/foods10102483