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Optimization of Candida rugosa lipase immobilization parameters on magnetic silica aerogel using adsorption method

Document Type : Full article

Authors

Sahand University of Technology

Abstract

Magnetic silica aerogel in hydrophobic and hydrophilic forms were used as support to immobilize Candida rugosa lipase by adsorption method. Response surface methodology (RSM) was employed to study the effects of the three most important immobilization parameters, namely enzyme/support ratio (0.3-0.5, w/w), immobilization time (60-120 min) and alcohol percentage (20-40, %v/v) on the specific activity of immobilized lipase on the hydrophobic supports. For hydrophilic supports, alcohol percentage was removed as there was no need for pre-wetting step in enzyme immobilization process. Second order regression models with high coefficient determination (R2) values of higher than 0.98 were fitted to predict the response as function of immobilization parameters. The results indicated that for hydrophobic supports, optimum values for enzyme/support ratio, immobilization time and alcohol percentage were obtained at 0.45 (w/w), 94.27 min and 38.81 %, respectively, in which specific activity were predicted at 15.32 U/mg-protein. For hydrophilic supports, the optimum enzyme/support ratio and immobilization time were predicted at 0.47 (w/w) and 83.47 min, respectively. Specific activity in these conditions were obtained 11.21 U/mg-protein. As the difference between the experimental and predicted values was showed as non-significant, the response surface models employed could be considered as adequate.

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References
Hasan, F. Shah, A. A. and Hameed, A., "Industrial applications of microbial lipases", Enzyme Microb. Technol., 39 (2), 235 (2006).
[2] Kapoor, M. and Gupta, M. N., "Lipase promiscuity and its biochemical applications", Process Biochem., 47 (4), 555 (2012).
[3] ­­Moussavou Mounguengui, R. W. Brunschwig, C. Barea, B. Villeneuve, P. and Blin, J., "Are plant lipases a promising alternative to catalyze transesterification for biodiesel production?", Prog. Energy Combust. Sci., 39 (5), 441 (2013).
[4] Liu, J. H. Zhang, Y. Y. Xia, Y. M. and Su, F., "Optimization of immobilization conditions of candida antarctica lipase based on response surface methodology", Chem. Biochem. Eng. Q, 24 (2), 203 (2010).
[5] Trbojevic, J. N. Dimitrijevic, A. S. Velickovic, D. V. Jankulovic, M. G. and Milosavic, N. B., "Isolation of Candida rugosa lipase isoforms", Hem. Ind., 67 (5), 703 (2013).
[6] Mateo, C. Palomo, J. M. Fernandez, L. G. Guisan, J. M. and Fernandez, L. R., "Improvement of enzyme activity, stability and selectivity via immobilization techniques", Enzyme Microb. Technol., 40 (6), 1451 (2007).
[7] Zhao, X. Qi, F. Yuan, C. Du, W. and Liu, D., "Lipase-catalyzed process for biodiesel production: enzyme immobilization, process simulation and optimization", Renew. Sust. Energ. Rev., 44, 182 (2015).
[8] Cambillau, C. and Tilbeurgh, H.v., "Structure of hydrolases: lipases and cellulases", Curr. Opin. Struct. Biol., 3 (6), 885 (1993).
[9] Talbert, J. N. and Goddard, J. M., "Enzymes on material surfaces", Colloids Surf. B Bio interfaces, 93, 8 (2012).
[10] Lee, D. G. Ponvel, K. M. Kim, M. Hwang, S. Ahn, I. S. and Lee, C. H., "Immobilization of lipase on hydrophobic nano-sized magnetite particles", J. Mol. Catal. B Enzym., 57 (1-4), 62 (2009).
[11] Kharrat, N. Ali, Y. B. Marzouk, S. Gargouri, Y. T. and Karra-Châabouni, M., "Immobilization of Rhizopus oryzae lipase on silica aerogels by adsorption: Comparison with the free enzyme", Process Biochem., 46 (5), 1083 (2011).
[12] Buisson, P. Hernandez, C. Pierre, M. and Pierre, A. C., "Encapsulation of lipases in aerogels", J. Non-Crys. Solids, 285 (1-3), 295 (2001).
[13] Maury, S. Buisson, P. and Pierre, A. C., "Porous texture modification of silica aerogels in liquid media and its effect on the activity of a lipase", Langmuir, 17 (21), 6443 (2001).
[14] Pierre, A. and Buisson, P., "Influence of the porous texture of silica gels on the enzymatic activity of lipases in esterification reactions", J. Mol. Catal. B Enzym., 11 (4-6), 639 (2001).
[15] Maury, S. Buisson, P. and Pierre, A. C., "Catalytic activity of Burkholderia (Pseudomonas) cepacia encapsulated in silica aerogels in esterification and hydrolysis as a function of the gel and solvent hydrophobicities", J. Mol. Catal. B Enzym., 19-20, 269 (2002).
[16] Rassy, E. Maury, H. Buisson, S. and Pierre, A. C., "Hydrophobic silica aerogel-lipase biocatalysts: Possible interactions between the enzyme and the gel", J. Non-Crys. Solids, 350, 23 (2004).
[17] Maury, S. Buisson, P. Perrard, A. and Pierre, A. C., "Compared esterification kinetics of the lipase from Burkholderia cepacia either free or encapsulated in a silica aerogel", J. Mol. Catal. B Enzym., 32 (5-6), 193 (2005).
[18] Karout, A. Buisson, P. Perrard, A. and Pierre, A. C., "Shaping and mechanical reinforcement of silica aerogel biocatalysts with ceramic fiber felts", J. Sol-Gel Sci. Technol., 36 (2), 163 (2005).
[19] Orcaire, O. Buisson, P. and Pierre, A. C., "Application of silica aerogel encapsulated lipases in the synthesis of biodiesel by transesterification reactions", J. Mol. Catal. B-Enzym., 42 (3-4), 106 (2006).
[20] Gao, S. Wang, Y. Wang, T. Luo, G. and Dai, Y., "Immobilization of lipase on methyl-modified silica aerogels by physical adsorption", Bioresour. Technol., 100 (2), 996 (2009).
[21] Bargozin, H. Amirkhani, L. Moghaddas, J. S. and Ahadian, M. M., "Synthesis and application of silica aerogel-MWCNT nanocomposites for adsorption of organic pollutants", Sci. Iran, 17 (2), 122 (2010).
[22] Shi, F. Wang, L. Liu, J. and Zeng, M., "Effect of heat treatment on silica aerogels prepared viaambient drying", J. Mater. Sci. Technol., 23 (3), 402 (2007).
[23] Kilinc, A. Teke, M. Onal, S. and Telefoncu, A., "Immobilization of pancreatic lipase on chitin and chitosan", Prep. Biochem. Biotech., 36 (2), 153 (2006).
[24] Chang, S. F. Chang, S. W. Yen, Y. H. and Shieh, C. J., "Optimum immobilization of Candida rugosa lipase on celite by RSM", Appl. Clay Sci., 37 (1-2), 67 (2007).
[25] Lowry, O. H. Rosebrough, N. J. Farr, A. L. and Randall, R. J., "Protein measurment with the folin phenol reagent", J. Biol. Chem., 193, 265 (1951).
[26] Anarjan, N. Jaberi, N. Yeganeh-Zare, S. Banafshehchin, E. Rahimirad, A. and Jafarizadeh-Malmiri, H., "Optimization of mixing parameters for α-tocopherol nanodispersions prepared using solvent displacement method", J. Am. Oil Chem.
Soc., 91 (8), 1397 (2014).
[27] Stober, W. Fink, A. and Bohn, E., "Controlled growth of monodisperse silica spheres in micron size range", J. Colloid Interf. Sci., 26 (1), 62 (1968).
[28] Chamorro, S. Sanchez-Montero, J. M. Alcantara, A. R. and Sinisterra, J. V., "Treatment of Candida rugosa lipase with short-chain polar organic solvents enhances its hydrolytic and synthetic activities", Biotechnol. Lett., 20 (5), 499 (1998).
[29] Blanco, R. M. Terreros, P. Munoz, N. and Serra, E., "Ethanol improves lipase immobilization on a hydrophobic support", J. Mol. Catal. B-Enzym., 47 (1-2), 13 (2007).
[30] Gao, S. Wang, W. Wang, Y. Luo, G. and Dai, Y., "Influence of alcohol treatments on the activity of lipases immobilized on methyl-modified silica aerogels", Bioresour. Technol., 101 (19), 7231 (2010).
[31] Talukder, M. M. R. Tamalampudy, S. Li, C. J. Yanglin, L. Wu, J. Kondo, A. and Fukuda, H., "An improved method of lipase preparation incorporating both solvent treatment and immobilization onto matrix", Biochem. Eng. J., 33 (1), 60 (2007).
 
Iranian Journal of Chemical Engineering(IJChE)
Volume 13, Issue 3
July 2016
Pages 19-31
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