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A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles

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DOI: 10.4236/gsc.2014.41003    3,524 Downloads   5,505 Views   Citations


Enantiopure epoxides and their corresponding chiral vicinal diols serve as valuable intermediates in the synthesis of biologically active pharma and agro-compounds and also value added fine chemicals. Biocatalysts are well known for their selective hydrolysis of racemic epoxides to give optically pure chiral diols. This study highlights an efficient process of synthesis of chiral vicinal diols in good yields and enantioselectiviy using horse radish peroxidase enzyme immobilized on the amine functionalized magnetic nano particles (Fe3O4 nanoparticles) as enzyme carriers. It also facilitates separation of MNP-immobilized enzymes by applying external magnetic field. The immobilization of magnetic nano particles was confirmed by transmission electron microscope (TEM) and scanning electron microscope (SEM). The MNP-immobilized peroxidase enzyme improved stability of the enzyme and has shown broader substrate specificity in enantioselective hydrolysis of racemic epoxides, under mild and environmentally friendly conditions. The methodology MNP-immobilized enzyme developed in the synthesis of chiral diols has a potential for use in large-scale applications.

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S. Siva Deepthi, E. Prasad, B. Venkata Subba Reddy, B. Sreedhar and A. Bhaskar Rao, "A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles," Green and Sustainable Chemistry, Vol. 4 No. 1, 2014, pp. 15-19. doi: 10.4236/gsc.2014.41003.


[1] W. J. Choi, “Biotechnological Production of Enantiopure Epoxides by Enzymatic Kinetic Resolution,” Applied Microbiology and Biotechnology, Vol. 84, No. 2, 2009, pp. 239-247.
[2] D. Sareen and R. Kumar, “Prospecting for Efficient Enantioselective Epoxide Hydrolases,” Indian Journal of Biotechnology, Vol. 10, 2011, pp. 161-177.
[3] C. Mateo, A. Archelas, R. Fernandez-Lafuente, J. M. Guisanb and R. Furstoss, “Enzymatic Transformations. Immobilized A. niger Epoxide Hydrolase as a Novel Biocatalytic Tool for Repeated-Batch Hydrolytic Kinetic Resolution of Epoxides,” Organic & Biomolecular Chemistry, Vol. 1, No. 15, 2003, pp. 2739-2743.
[4] W. Adam, M. Lazarus, C. R. Saha-Moller, O. Weichold, U. Hoch, D. Haring and P. Schreier, “Biotransformations with Peroxidases,” Advances in Biochemical Engineering/ Biotechnology, Vol. 63, 1999, pp. 73-108.
[5] H. Lin, J. Y. Liu, H. B. Wang, A. A. Q. Ahmed and Z. L. Wu, “Biocatalysis as an Alternative for the Production of Chiral Epoxides: A Comparative Review,” Journal of Molecular Catalysis B: Enzymatic, Vol. 72, No. 3-4, 2011, pp. 77-89.
[6] Y. Genzel, A. Archelas, Q. B. Broxterman, B. Schulze and R. Furtoss, “Microbiological Transformations. 47. A Step toward a Green Chemistry Preparation of Enantiopure (S)-2-,3-Pyridyloxirane via an Epoxide Hydrolase Catalyzed Kinetic Resolution,” The Journal of Organic Chemistry, Vol. 66, No. 2, 2001, pp. 538-543.
[7] S. Colonna, N. Gaggero, C. Richelmi and P. Pasta, “Recent Biotechnological Developments in the Use of Peroxidases,” Trends in Biotechnology, Vol. 17, No. 4, 1999, 163-168.
[8] A. J. Carlsson, P. Bauer, H. Ma and M. Widersten, “Obtaining Optical Purity for Product Diols in Enzyme Catalyzed Epoxide Hydrolysis: Contributions from Changes in Both Enantio- and Regioselectivity,” Biochemistry, Vol. 51, No. 38, 2012, pp. 7627-7637.
[9] N. S. Finney, “Enantioselective Epoxide Hydrolysis: Catalysis Involving Microbes, Mammals and Metals,” Chemistry and Biology, Vol. 5, No. 4, 1998, pp. 73-79.
[10] H. C. Zhou, W. Li, Q. H. Shou, H. S. Gao, P. Xu, F. L. Deng and H. Z. Liu, “Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids,” Chinese Journal of Chemical Engineering, Vol. 20, No. 1, 2012, pp. 146-151.
[11] P. A. Johnson, H. J. Park and A. J. Driscoll, “Enzyme Nanoparticle Fabrication: Magnetic Nanoparticle Synthesis and Enzyme Immobilization,” Methods in Molecular Biology, Vol. 679, 2011, pp. 183-191.
[12] Y. Ren, J. G. Rivera, L. He, H. Kulkarni, D. K. Lee and P. B. Messersmith, “Facile, High Efficiency Immobilization of Lipase Enzyme on Magnetic Iron Oxide Nanoparticles via Biomimetic Coating,” BMC Biotechnology, Vol. 11, 2011, pp. 63-70.
[13] A. Dyal, K. Loos, M. Noto, S. W. Chang, C. Spagnoli, K. V. P. M. Shafi, A. Ulman, M. Cowman and R. A. Gross, “Activity of Candida rugosa Lipase Immobilized on g-Fe2O3 Magnetic Nanoparticles,” Journal of the American Chemical Society, Vol. 125, No. 7, 2003, pp. 1684-1685.
[14] C. G. C. M. Netto, H. E. Tomo and L. H. Andrade, “Superparamagnetic Nanoparticles as Versatile Carriers and Supporting Materials for Enzymes,” Journal of Molecular Catalysis B: Enzymatic, Vol. 85-86, 2013, pp. 71-92.
[15] L. Zhou, J. Yuan and Y. Wei, “Core-Shell Structural Iron Oxide Hybrid Nanoparticles: From Controlled Synthesis to Biomedical Applications,” Journal of Materials Chemistry, Vol. 21, 2011, pp. 2823-2840.
[16] A. K. Johnson, A. M. Zawadzka, L. A. Deobald, R. L. Crawford and A. J. Paszczynski, “Novel Method for Immobilization of Enzymes to Magnetic Nanoparticles,” Journal of Nanoparticle Research, Vol. 10, 2008, pp. 1009-1025.
[17] H. M. R. Gardimalla, D. Mandal, P. D. Stevens, M. Yen and Y. Gao, “Superparamagnetic Nanoparticle-Supported Enzymatic Resolution of Racemic Carboxylates,” Chemical Communications, No. 35, 2005, pp. 4432-4434.
[18] J. Wang, G. Meng, K. Tao, M. Feng, X. Zhao, Z. Li, H. Xu, D. Xia and J. R. Lu, “Immobilization of Lipases on Alkyl Silane Modified Magnetic Nanoparticles: Effect of Alkyl Chain Length on Enzyme Activity,” Plos One, Vol. 7, No. 8, 2012, Article ID: e43478.
[19] F. Mahdizadeh, A. Karimi and L. Ranjbarian, “Immobilization of Glucose Oxidase on Synthesized Superparamagnetic Fe3O4 Nanoparticles; Application for Water Deoxygenation,” International Journal of Scientific & Engineering Research, Vol. 3, No. 5, 2012, pp. 1-6.
[20] J. Xu, C. Ju, J. Sheng, F. Wang, Q. Zhang, G. Sun and M. Sun, “Synthesis and Characterization of Magnetic Nanoparticles and Its Application in Lipase Immobilization,” Bulletin of the Korean Chemical Society, Vol. 34, No. 8, 2013, pp. 2408-2412.
[21] X. Zheng, S. Luo, L. Zhang and J. P. Cheng, “Magnetic Nanoparticle Supported Ionic Liquid Catalysts for CO2 Cycloaddition Reactions,” Green Chemistry, Vol. 11, No. 4, 2009, pp. 455-458.
[22] K. Khoshnevisana, A. K. Bordbarb, D. Zarec, D. Davoodic, M. Noruzic, M. Barkhic and M. Tabatabaei, “Immobilization of Cellulose Enzyme on Superparamagnetic Nanoparticles and Determination of Its Activity and Stability,” Chemical Engineering Journal, Vol. 171, No. 2, 2011, pp. 669-673.
[23] Y. Kim, I. Lee, S. Choi, O. Lee, J. Shim, J. Lee, J. Kim abd E. Y. Lee, “Enhanced Stability and Reusability of Marine Epoxide Hydrolase Using Ship-in-a-Bottle Approach with Magnetically-Separable Mesoporous Silica,” Journal of Molecular Catalysis B: Enzymatic, Vol. 89, 2013, pp. 48-51.
[24] K. Pospiskova and I. Safarik, “Low-Cost, Easy-to-Prepare Magnetic Chitosan Microparticles for Enzymes Immobilization,” Carbohydrate Polymers, Vol. 96, No. 2, 2013, pp. 545-548.
[25] B. Chance and A. C. Maehly, “Assay of Catalases and Peroxidases,” Methods in Enzymology, Vol. 2, 1955, pp. 773-775.

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