Functionalization of Mesoporous SBA-15 with APTES by Co-Condensation and its Effect on Immobilization of Candida rugosa Lipase

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Abstract:

Functionalized SBA-15 with mesoscopic pore channels was synthesized by co-condensation of tetraethoxysilane and (3-aminopropyl) triethoxysilane (APTES) via hydrothermal process. Small-angle X-ray powder diffraction, scanning electron microscopy and transmission electron microscopy were used to monitor the effect of surface functionalization on the structural and textural features of the SBA-15. The results suggested that the structural ordering of functionalized SBA-15, as well as pore diameters, pore volumes and surface areas, were decreased with increasing the APTES molar ratio. Candida rugosa lipase (CRL) was used as a model enzyme for studying the effect of amino-functionalized on loading amount and enzymatic activity. The effects of pH and temperature on catalytic hydrolysis of tributyrin by immobilized CRL were investigated. The results showed that immobilized CRL had a well adaptability in a wide pH and temperature region, and CRL immobilized on functionalized SBA-15 exhibited much higher enzymatic activity than free CRL, especially, 5 mol% APTES functionalized SBA-15 immobilized CRL displayed the highest activity.

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Key Engineering Materials (Volumes 645-646)

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1261-1266

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May 2015

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[1] S.P. Hudson, R.F. Padera, R. Langer, D.S. Kohane, Biomaterials 29 (2008) 4045–4055.

DOI: 10.1016/j.biomaterials.2008.07.007

Google Scholar

[2] Z.A. AlOthman, A.W. Apblett, Appl. Surf. Sci. 256 (2010) 3573–3580.

Google Scholar

[3] G.W. Zhou, Y.J. Chen, S.H. Yang, Micropor. Mesopor. Mater. 119 (2009) 223–229.

Google Scholar

[4] L.F. Giraldo, B.L. López, L. Pérez, S. Urrego, L. Sierra, M. Mesa, Macromol. Symp. 258 (2007) 129–141.

DOI: 10.1002/masy.200751215

Google Scholar

[5] M. ΙΙ Kim, J. Kim, J. Lee, S. Shin, H.B. Na, T. Hyeon, H.G. Park, H.N. Chang, Micropor. Mesopor. Mater. 111 (2008) 18–23.

Google Scholar

[6] R.A. Sheldon, Adv. Synth. Catal. 349 (2007) 1289–1307.

Google Scholar

[7] X.A. Zhang, W.J. Wu, J.F. Wang, X.Z. Tian, Appl. Surf. Sci. 254 (2008) 2893–2899.

Google Scholar

[8] X.H. Zhang, W.Y. Zhang, J.P. Li, N. Zhao, W. Wei, Y.H. Sun, Catal. Commun. 8 (2007) 437–441.

Google Scholar

[9] A. Sayari, B.H. Han, Y. Yang, J. Am. Chem. Soc. 126 (2004) 14348–14349.

Google Scholar

[10] H. Ma, J. He, D.G. Evans, X. Duan, J. Mol. Catal. B: Enzym. 30 (2004) 209–217.

Google Scholar

[11] H. Zhang, J.M. Sun, D. Ma, X.H. Bao, A. Klein-Hoffmann, G. Weinberg, D.S. Su, R. Schlögl, J. Am. Chem. Soc. 126 (2004) 7440–7441.

DOI: 10.1021/ja048630e

Google Scholar

[12] A. Macario, M. Moliner, A. Corma, G. Giordano, Micropor. Mesopor. Mater. 118 (2009) 334–340.

Google Scholar

[13] A.Z. Abdullah, N.S. Sulaiman, A.H. Kamaruddin, Biochem. Eng. J. 44 (2009) 263–270.

Google Scholar