화학공학소재연구정보센터
Journal of Industrial and Engineering Chemistry, Vol.35, 224-230, March, 2016
Thiol and urea functionalized magnetic nanoparticles with highly enhanced loading capacity and thermal stability for lipase in transesterification
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Magnetic nanoparticles (MNPs) were prepared by a co-precipitation method and thiol and urea functionalized using (3-mercaptopropyl) trimethoxysilane (MPTS) and 1-(3-trimethoxysilyl propyl) urea (TMSPU). The samples were characterized by SEM, XRD and FTIR, and BET surface area measurement and used for immobilization of Candida rugosa lipase type VII (CRL7) and Thermomyces lanuginosus lipase (TLL) for a transesterification reaction. The loading capacities of the lipases immobilized on the functionalized MNPs were also studied. The activity and thermal stability of the immobilized lipases were compared to those of the free enzymes too. The loading capacities of CRL7 and TLL on MNPs-TMSPU are 410 and 440 mg/g-MNPs, 5.9 and 5.5 times higher than those on the unfunctionalized MNPs, respectively. The initial activities of both CRL7 and TLL on MNPs-TMSPU are higher than those on MNPs-MPTS. After 30 min incubation at 80 ℃, the remained activity of TLL on MNPs-TMSPU is 2.5 times higher than that of the free enzyme. The remained activities of the biocomposites assayed after each use in transesterification reaction demonstrate that TLL-MNPs-TMSPU biocomposite has a high yield of 92%. The immobilized TLL on MNPs-TMSPU and MPTS retain 80% and 70% of their initial activities after 8 times reuse, respectively. The functionalized MNPs are magnetically separated for reuse.
  1. Reetz MT, Zonta A, Vijayakrishnan V, Schimossek K, J. Mol. Catal. A-Chem., 134, 251 (1998)
  2. Drauz K, Enzyme Catalysis in Organic Synthesis: A Comprehensive Handbook, John Wiley & Sons, 2012.
  3. Perez VH, da Silva GS, Gomes FM, de Castro HF, Biochem. Eng. J., 34, 13 (2007)
  4. Szczesna-Antczak M, Kubiak A, Antczak T, Bielecki S, Renew. Energy, 34(5), 1185 (2009)
  5. Ren Y, Rivera J, He L, Kulkarni H, Lee DK, Messersmith P, BMC Biotechnology, 11, 1 (2011)
  6. Fernandez-Lafuente R, J. Mol. Catal. B-Enzym., 62, 197 (2010)
  7. Aravindan R, Anbumathi P, Viruthagiri T, Indian J. Biotechnol., 6, 141 (2007)
  8. Zhang DH, Yuwen LX, Xie YL, Li W, Li XB, Colloids Surf. B: Biointerfaces, 89, 73 (2012)
  9. Jainae K, Sukpirom N, Fuangswasdi S, Unob F, J. Ind. Eng. Chem., 23, 273 (2015)
  10. Ribeiro BD, Castro AMD, Coelho MAZ, Freire DMG, Enzyme Res., 2011 (2011)
  11. Sheldon RA, Adv. Synth. Catal., 349, 1289 (2007)
  12. Brady D, Jordaan J, Biotechnol. Lett., 31(11), 1639 (2009)
  13. Polizzi KM, Bommarius AS, Broering JM, Chaparro-Riggers JF, Curr. Opin. Chem. Biol., 11, 220 (2007)
  14. Minovska V, Winkelhausen E, Kuzmanova S, J. Serb. Chem. Soc., 70, 609 (2005)
  15. Murty VR, Bhat J, Muniswaran P, Biotechnol. Bioprocess Eng., 7, 57 (2002)
  16. Chiou SH, Wu WT, Biomaterials, 25, 197 (2004)
  17. Verma ML, Naebe M, Barrow CJ, Puri M, PLOS ONE, 8, e73642 (2013)
  18. Ponvel KM, Lee DG, Woo EJ, Ahn IS, Lee CH, Korean J. Chem. Eng., 26(1), 127 (2009)
  19. Gurunathan S, J. Ind. Eng. Chem. (2015)
  20. Ballav N, Choi HJ, Mishra SB, Maity A, J. Ind. Eng. Chem., 20(6), 4085 (2014)
  21. Faraji M, Yamini Y, Rezaee M, J. Iran. Chem. Soc., 7, 1 (2010)
  22. Lin CC, Ho JM, Hsieh HL, Chem. Eng. J., 203, 88 (2012)
  23. Lim CW, Lee IS, Nano Today, 5(5), 412 (2010)
  24. Netto CG, Toma HE, Andrade LH, J. Mol. Catal. B-Enzym., 85, 71 (2013)
  25. Arkles B, Silane Coupling Agents: Connecting Across Boundaries, Gelest, Morrisville, 2004, pp. 1-5.
  26. Wang J, Meng G, Tao K, Feng M, Zhao X, Li Z, Xu H, Xia D, Lu JR, PLoS ONE, 7, e43478 (2012)
  27. Marszall MP, Siodmiak T, Catal. Commun., 24, 80 (2012)
  28. Ghasemi S, Heidary M, Faramarzi MA, Habibi Z, J. Mol. Catal. B-Enzym., 100, 121 (2014)
  29. Meng X, Xu G, Zhou QL, Wu JP, Yang LR, Food Chem., 143, 319 (2014)
  30. Jiang W, Yang HC, Yang SY, Horng HE, Hung JC, Chen YC, Hong CY, J. Magn. Magn. Mater., 283, 210 (2004)
  31. Bach LG, Islam MR, Kim JT, Seo S, Lim KT, Appl. Surf. Sci., 258(7), 2959 (2012)
  32. Kanimozhi S, Perinbam K, Mater. Res. Bull., 48(5), 1830 (2013)
  33. Khoobi M, Motevalizadeh SF, Asadgol Z, Forootanfar H, Shafiee A, Faramarzi MA, Biochem. Eng. J., 88, 131 (2014)
  34. Ren Y, Rivera JG, He L, Kulkarni H, Lee DK, Messersmith PB, BMC Biotechnology, 11, 63 (2011)
  35. Han D, Walde P, Luisi PL, Biocatal. Biotransform., 4, 153 (1990)
  36. Rodrigues RC, Ayub MAZ, Process Biochem., 46, 682 (2011)
  37. Vasudevan PT, Fu B, Waste Biomass Valorization, 1, 47 (2010)
  38. Waldron RD, Phys. Rev., 99, 1727 (1955)
  39. Tran HV, Tran LD, Nguyen TN, Mater. Sci. Eng. C-Biomimetic Supramol. Syst., 30, 304 (2010)
  40. Ma M, Zhang Y, Yu W, Shen HY, Zhang HQ, Gu N, Colloids Surf. A: Physicochem. Eng. Asp., 212, 219 (2003)
  41. Guang-She L, Li-Ping L, Smith RL, Inomata H, J. Mol. Struct., 560, 87 (2001)
  42. White LD, Tripp CP, J. Colloid Interface Sci., 232(2), 400 (2000)
  43. Yamaura M, Camilo R, Sampaio L, Macedo M, Nakamura M, Toma H, J. Magn. Magn. Mater., 279, 210 (2004)
  44. Bini RA, Marques RFC, Santos FJ, Chaker JA, Jafelicci M, J. Magn. Magn. Mater., 324, 534 (2012)
  45. Li SF, Wu WT, Biochem. Eng. J., 45, 48 (2009)
  46. Patel V, Gajera H, Gupta A, Manocha L, Madamwar D, Biochem. Eng. J., 95, 62 (2015)
  47. Liu X, Lei L, Li Y, Zhu H, Cui Y, Hu H, Biochem. Eng. J., 56, 142 (2011)
  48. Dizge N, Keskinler B, Tanriseven A, Biochem. Eng. J., 44, 220 (2009)
  49. Roger AS, ChemInform, 38 (2007)
  50. Murty VR, Bhat J, Muniswaran PKA, Biotechnol. Bioprocess Eng., 7, 57 (2002)
  51. Lee DG, Ponvel KM, Kim M, Hwang S, Ahn IS, Lee CH, J. Mol. Catal. B-Enzym., 57, 62 (2009)
  52. Yilmaz E, Sezgin M, Yilmaz M, J. Mol. Catal. B-Enzym., 69, 35 (2011)
  53. Chalkias N, Immobilization of enzymes on inorganic nanoparticles, (PhD diss.), Cornell University, 2007.
  54. Fjerbaek L, Christensen KV, Norddahl B, Biotechnol. Bioeng., 102(5), 1298 (2009)
  55. S.L. Sigma lipase assay. Sigma bulletin No 800. Sigma, MO.