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Enhanced hydroxylation of imidacloprid by Stenotrophomonas maltophilia upon addition of sucrose

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Abstract

Sucrose’s ability to promote the hydroxylation of imidacloprid (IMI) by bacterium Stenotrophomonas maltophilia strain CGMCC 1.1788 was examined. Both growing culture and resting cells could transform IMI into 5-hydroxy IMI. Adding 2% sucrose to the growing culture transformation broth and 5% sucrose to the resting cell transformation broth resulted in biotransformation yields, respectively, 2.5 and 9 times greater than without sucrose. In the growing culture transformation, sucrose increased biomass, which led to enhance hydroxylation of IMI. In the resting cell transformation, sucrose was used not as a carbon source but as an energy source for cofactor regeneration for hydroxylation of IMI. The hydroxylation activity of IMI was promoted eightfold by adding reduced nicotinamide adenine dinucleotide (NADH) to the cell-free extract. The hydroxylation of IMI was significantly inhibited by P450 inhibitor piperonyl butoxide. It seems that the hydroxylation of IMI by S.maltophilia CGMCC 1.1788 might proceed through a system by cooperating with P450 enzyme.

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References

  • Asperger O, Steinbrenner H, Lehmann A, Petsch M, Griengl H (1999) Induction and functional role of cytochromes P450 in the filamentous fungi Mortierella alpine ATCC 8979 and Cunninghamella blakesleeana DSM 1906 during hydroxylation of cycloalkylbenzoxazoles. Appl Microbiol Biotechnol 51:516–522

    Article  CAS  Google Scholar 

  • Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248–254

    CAS  PubMed  Google Scholar 

  • Dai YJ, Yuan S, Ge F, Chen T, Xu SC, Ni JP (2006) Microbial hydroxylation of imidacloprid for the synthesis of highly insecticidal olefin imidacloprid. Appl Microbiol Biotechnol 71:927–934

    Article  CAS  PubMed  Google Scholar 

  • Dick R, Kanne D, Casida J (2005) Identification of aldehyde oxidase as the neonicotinoid nitroreductase. Chem Res Toxicol 18:317–323

    Article  CAS  PubMed  Google Scholar 

  • Ernst M, Kaup B, Müller M, Bringer-Meyer S, Sahm H (2005) Enantioselective reduction of carbonyl compounds by whole-cell biotransformation, combining a formate dehydrogenase and a (R)-specific alcohol dehydrogenase. Appl Microbiol Biotechnol 66:629–634

    Article  CAS  PubMed  Google Scholar 

  • Grosse S, Laramee L, Wendlandt K, Mcdonald I, Miguez C, Kleber H (1999) Purification and characterization of the soluble methane monooxygenase of the type II methanotrophic bacterium Methylocystis sp. Appl Environ Microbiol 65:3929–3935

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Holland H, Weber H (2000) Enzymatic hydroxylation reactions. Curr Opin Biotechnol 11:547–553

    Article  CAS  PubMed  Google Scholar 

  • Kagabu S, Kato C, Nishimura K (2004) Insecticidal and neuroblocking activities toward American cockroach (Periplaneta americana L.) of imidacloprid metabolites, 5-hydroxy-, 4, 5-dihydroxy- and 4,5-dehydroimidacloprid. J Pestic Sci 29:376–379

    Article  CAS  Google Scholar 

  • Krohn J, Hellpointner E (2002) Environmental fate of imidacloprid. Pflanzenschutz-Nachrichten Bayer 55 special edition:3–26

    CAS  Google Scholar 

  • Lee N-R, Hwang M-O, Jung G-H, Kim Y-S, Min K-H (1996) Physical structure and expression of alkBA encoding alkane hydroxylase and rubredoxin reductase from Pseudomonas maltophilia. Biochem Biophys Res Commun 218:17–21

    Article  CAS  PubMed  Google Scholar 

  • Lewis D, Hlavica P (2000) Interactions between redox partners in various cytochrome P450 systems: functional and structural aspects. Biochim Biophys Acta 1460:353–374

    Article  CAS  PubMed  Google Scholar 

  • Matsuzaki F, Wariishi H (2004) Functional diversity of cutochrome P450s of the white-rot fungus Phanerochaete chrysosporium. Biochem Biophys Res Commun 324:387–393

    Article  CAS  PubMed  Google Scholar 

  • Nagasawa T, Hurh B, Yamamne T (1994) Production of 6-hydroxynicotinic acid from nicotinic acid by resting cells of Pseudomonas fluorescens TN5. Biosci Biotech Biochem 58:665–668

    Article  CAS  Google Scholar 

  • Nauen R, Tietjen K, Wagner K, Elbert A (1998) Efficacy of plant metabolites of imidacloprid against Myzus persicae and Aphis gossypii (Homoptera: Aphididae). Pestic Sci 52:53–57

    Article  CAS  Google Scholar 

  • Nauen R, Rechmann U, Armborst S, Stupp HP, Elbert A (1999) Whitefly-active metabolites of imidacloprid: biological efficacy and translocation in cotton plants. Pestic Sci 55:265–271

    Article  CAS  Google Scholar 

  • Nauen R, Ebbinghaus-Kintscher U, Schmuck R (2001) Toxicity and nicotinic acetylcholine receptor interaction of imidacloprid and its metabolites in Apis mellifera (Hymenoptera: Apidae). Pest Manag Sci 57:577–586

    Article  CAS  PubMed  Google Scholar 

  • Sachan A, Ghosh S, Mitra A (2006) Biotransformation of p-coumaric acid by Paecilomyces variotii. Lett Appl Microbiol 42:35–41

    Article  CAS  PubMed  Google Scholar 

  • Schulz-Jander D, Casida J (2002) Imidacloprid insecticide metabolism: human cytochrome P450 isozymes differ in selectivity for imidazolidine oxidation versus nitroimine reduction. Toxicol Lett 132:65–70

    Article  CAS  PubMed  Google Scholar 

  • Uchida A, Yoshida T, Ogawa M, Nagasawa T (2003) Regioselective hydroxylation of quinolinic acid, lutidinic acid and isocinchomeronic acid by resting cells of pyridine dicarboxylic acid-degrading microorganisms. Appl Microbiol Biotechnol 62:337–341

    Article  CAS  PubMed  Google Scholar 

  • Urlacher V, Lutz-Wahl S, Schmid R (2004) Microbial P450 enzymes in biotechnology. Appl Microbiol Biotechnol 64:317–325

    Article  CAS  PubMed  Google Scholar 

  • Yuan S, Yang Y, Sun J, Liang MX, Dai YJ, Zhang XN, Xu SC (2005) A combined process of hydroxylation of nicotinic acid by growing culture and hydroxylation of 3-cyanopyridine by resting cells of Comamonas testosteroni JA1. Eng Life Sci 5:369–374

    Article  CAS  Google Scholar 

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Acknowledgment

We are thankful for the support from the Natural Science Foundation of Jiangsu, China (BK2006574), the Key Basic Research Program of the Jiangsu Higher Education Institutions of China (06KJA21016), and the Natural Science Foundation of the Jiangsu Higher Education Institutions of China (04KJB180071).

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Correspondence to Sheng Yuan.

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Dai, Yj., Chen, T., Ge, F. et al. Enhanced hydroxylation of imidacloprid by Stenotrophomonas maltophilia upon addition of sucrose. Appl Microbiol Biotechnol 74, 995–1000 (2007). https://doi.org/10.1007/s00253-006-0762-2

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  • DOI: https://doi.org/10.1007/s00253-006-0762-2

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