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Effect of Extracellular Tyrosinase on the Expression Level of P450, Fpr, and Fdx and Ortho-hydroxylation of Daidzein in Streptomyces avermitilis

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Abstract

We have reported that the expression of CYP105D7 in Streptomyces avermitilis produces 112.5 mg L−1 of 7,3′,4′-trihydroxyisoflavone (3'ODI) in 15 h of the reaction time, when 7,4′-dihydroxyisoflavone (daidzein) is used as a substrate. Although production is significant, rapid degradation of 3'ODI after 15 h was observed in a whole-cell biotransformation system, suggesting the further modification of 3'ODI by endogenous enzymes. In this present study, the effect of deletion of extracellular tyrosinase (melC2) in S. avermitilis for 3'ODI production as well as the expressions of CYP105D7, ferredoxin (Fdx), and ferredoxin reductase (Fpr) were investigated. The result revealed that daidzein hydroxylation activity in the ∆melC2 mutant decreased by 40% compared with wild-type S. avermitilis. Further, melC2 deletion significantly affects the messenger RNA (mRNA) expression profile of CYP105D7 and its electron transfer counterparts. Real-time PCR analysis of 9 Fdx, 6 Fpr, and CYP105D7 revealed a significant decrease in mRNA expression level compared to wild-type S. avermitilis. The result clearly shows that the decrease in daidzein hydroxylation activity is due to the lower expression level of CYP105D7 and its electron transfer counterpart in the ∆melC2 mutant. Furthermore, melC2 deletion prevents the degradation of 3'ODI.

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References

  1. Murakami, T., Burian, J., Yanai, K., Bibb, M. J., & Thompson, C. J. (2011). A system for the targeted amplification of bacterial gene clusters multiplies antibiotic yield in Streptomyces coelicolor. Proceedings of the National Academy of Sciences of the United States of America, 108, 16020–16025.

    Article  CAS  Google Scholar 

  2. Roh, C., et al. (2009). Regioselective hydroxylation of isoflavones by Streptomyces avermitilis MA-4680. Journal of Bioscience and Bioengineering, 108, 41–46.

    Article  CAS  Google Scholar 

  3. Pandey, B. P., Lee, N., Choi, K. Y., Kim, J. N., Kim, E. J., & Kim, B. G. (2014). Identification of the specific electron transfer proteins, ferredoxin, and ferredoxin reductase, for CYP105D7 in Streptomyces avermitilis MA4680. Applied Microbiology and Biotechnology, 98, 5009–5017.

    Article  CAS  Google Scholar 

  4. Gan, H. M., Ibrahim, Z., Shahir, S., & Yahya, A. (2011). Identification of genes involved in the 4-aminobenzenesulfonate degradation pathway of Hydrogenophaga sp. PBC via transposon mutagenesis. FEMS Microbiology Letters, 318, 108.

    Article  CAS  Google Scholar 

  5. Fairhead, M., & Thöny-Meyer, L. (2012). Bacterial tyrosinases: old enzymes with new relevance to biotechnology. New Biotechnology, 29, 183–191.

    Article  CAS  Google Scholar 

  6. Claus, H., & Decker, H. (2006). Bacterial tyrosinases. Systematic and Applied Microbiology, 29, 3–14.

    Article  CAS  Google Scholar 

  7. García-Molina, F., et al. (2007). A review on spectrophotometric methods for measuring the monophenolase and diphenolase activities of tyrosinase. J Argic Food Chem, 55, 9739–9749.

    Article  Google Scholar 

  8. Gowda, L. R., & Paul, B. (2002). Diphenol activation of the monophenolase and diphenolase activities of field bean (Dolichos lablab) polyphenol oxidase. Journal of Agricultural and Food Chemistry, 50, 1608–1614.

    Article  CAS  Google Scholar 

  9. Omura, S., et al. (2001). Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites. Proceedings of the National Academy of Sciences of the United States of America, 98, 12215–12220.

    Article  CAS  Google Scholar 

  10. Lee, N., Kim, E. J., & Kim, B. G. (2012). Regioselective hydroxylation of trans-resveratrol via inhibition of tyrosinase from Streptomyces avermitilis MA4680. ACS Chemical Biology, 7, 1687–1692.

    Article  CAS  Google Scholar 

  11. Stutzman-Engwall K, Krebber A, Gustafsson C, Minshull J, Raillard S, Kim S, Chen Y. (2006). Methods related to Streptomyces avermitilis gene directed the ration of B2:B1 avermectin. U.S. paten 7, 029, 887 B2.

  12. Alison, B. A., Collier, L. S., Neidle, E. L., & Moran, M. A. (2000). Key aromatic-ring-cleaving enzyme, protocatechuate 3, 4-dioxygenase, in the ecologically important marine Roseobacter lineage. Applied and Environmental Microbiology, 66, 4662–4672.

    Article  Google Scholar 

  13. Lee, N., Lee, S-H., Baek, K., Kim, B-G., (2015). Heterologous expression of tyrosinase (Mel C2) from Streptomyces avermitilis MA4680 in E. coli and its application for ortho-hydroxylation of resveratrol to produce piceatannol. Applied Microbiol Biotechnol,

  14. Chang, T-S., Ding, H-Y., Tai, S.S-K., Wu, C-Y., 2007. Mushroom tyrosinase inhibitory effects of isoflavones isolated from soygerm koji fermented with aspergillus oryzae BCRC 32288. Food Chemistry, 105, 1430–1438.

  15. Nguyen, M. H., Nguyen, H. X., Nguyen, M. T., & Nguyen, N. T. (2012). Phenolic constituents from the heartwood of Artocapus altilis and their tyrosinase inhibitory activity. Natural Product Communications, 7, 185–186.

    CAS  Google Scholar 

  16. Zhang, H., Wang, Y., & Pfeifer, B. A. (2008). Bacterial hosts for natural product production. Molecular Pharmaceutics, 5, 212–225.

    Article  CAS  Google Scholar 

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Acknowledgements

The authors would like to acknowledge the Department of Chemical Science and Engineering, Kathmandu University, for providing basic support to conduct this research.

Funding

This research was supported by the National Research Foundation (NRF) of Korea funded by the Ministry of Science, ICT & Future Planning (2016953757).

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Authors and Affiliations

  1. Department of Chemical Science and Engineering, Kathmandu University, P.O.Box: 6250, Dhulikhel, Kavre, Nepal

    Bishnu Prasad Pandey

  2. School of Chemical and Biological Engineering, Institute of Molecular Biology and Genetics, Institute of Bioengineering, Seoul National University, Seoul, South Korea

    Nahum Lee & Byung-Gee Kim

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  1. Bishnu Prasad Pandey
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  2. Nahum Lee
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  3. Byung-Gee Kim
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Correspondence to Bishnu Prasad Pandey.

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Pandey, B.P., Lee, N. & Kim, BG. Effect of Extracellular Tyrosinase on the Expression Level of P450, Fpr, and Fdx and Ortho-hydroxylation of Daidzein in Streptomyces avermitilis . Appl Biochem Biotechnol 184, 1036–1046 (2018). https://doi.org/10.1007/s12010-017-2606-1

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