Activity and stability of bacterial cellulase immobilized on magnetic nanoparticles

doi:10.1016/S1872-2067(16)62487-7

Chinese Journal of Catalysis ›› 2016, Vol. 37 ›› Issue (11): 1891-1898.DOI: 10.1016/S1872-2067(16)62487-7

• Article • Previous Articles Next Articles

Activity and stability of bacterial cellulase immobilized on magnetic nanoparticles

Kandasamy Selvam, Muthusamy Govarthanan, Duraisamy Senbagam, Seralathan Kamala-Kannan, Balakrishnan Senthilkumar, Thangasamy Selvankumar

a Centre for Biotechnology, Muthayammal College of Arts and Science, Rasipuram, Namakkal 637408, Tamil Nadu, India;
b PG and Research Department of Biotechnology, Mahendra Arts and Science College (Autonomous), Kalippatti, Namakkal 637501, Tamil Nadu, India;
c Department of Applied Sciences, College of Environmental Technology, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050-8585, Japan;
d Department of Marine Biotechnology, Bharathidasan University, Tiruchirappalli 620024, Tamil Nadu, India;
e Division of Biotechnology, Advanced Institute of Environment and Bioscience, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan 570752, South Korea;
f Department of Medical Microbiology, College of Health and Medical Sciences, Haramaya University, P.O. Box 235, Harar, Ethiopia

Received:2016-05-08 Revised:2016-06-14 Online:2016-11-25 Published:2016-11-25
Contact: Balakrishnan Senthilkumar,E-mail:nbsenthilkumar@gmail.com;Thangasamy Selvankumar,Tel:+91-9443286292, +91-9443470394; E-mail:t_selvankumar@yahoo.com

Abstract

Abstract:

Magnetic nanoparticles (Fe₃O₄) were synthesized by co-precipitating Fe²⁺ and Fe³⁺ ions in an am-monia solution and treating under hydrothermal conditions. Cellulase was immobilized onto Fe₃O₄ magnetic nanoparticles via glutaraldehyde activation. Using response surface methodology and Box-Behnken design, the variables such as magnetic nanoparticle concentration, glutaraldehyde concentration, enzyme concentration, and cross linking time were optimized. The Box-Behnken design analysis showed a reasonable adjustment of the quadratic model with the experimental data. Statistical contour plots were generated to evaluate the changes in the response surface and to understand the relationship between the nanoparticles and the enzyme activity. Scanning electron microscopy, X-ray diffraction analysis, and Fourier transform infrared spectroscopy were studied to characterize size, structure, morphology, and binding of enzyme onto the nanoparticles. The stabil-ity and activity of the bound cellulase was analyzed using various parameters including pH, tem-perature, reusability, and storage stability. The immobilized cellulase was compared with free cel-lulase and it shows enhanced stability and activity.

Key words: Magnetic nanoparticle, Immobilized enzyme, Response surface methodology, Characterization

Kandasamy Selvam, Muthusamy Govarthanan, Duraisamy Senbagam, Seralathan Kamala-Kannan, Balakrishnan Senthilkumar, Thangasamy Selvankumar. Activity and stability of bacterial cellulase immobilized on magnetic nanoparticles[J]. Chinese Journal of Catalysis, 2016, 37(11): 1891-1898.

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References

[1] M. Vellard, Curr. Opin. Biotechnol., 2003, 14, 444-450.
[2] C. Zhang, S. K. Kim, Adv. Food Nutr. Res., 2012, 65, 423-435.
[3] V. Bulmus, K. Kesenci, E. Piskin, React. Funct. Polym., 1998, 38, 1-9.
[4] L. Cao, L. van Langen, R. A. Sheldon, Curr. Opin. Biotechnol., 2003, 14, 387-394.
[5] W. Tischer, F. Wedekind, Top. Curr. Chem., 1999, 200, 95-126.
[6] U. T. Bornscheuer, Angew. Chem. Int. Ed., 2003, 42, 3336-3337.
[7] B. C. Kim, S. Nair, J. Kim, J. H. Kwak, J. W. Grate, S. H. Kim, M. B. Gu, Nanotechnolgy, 2005, 16, S382-S388.
[8] H. F. Jia, G. Y. Zhu, B. Vugrinovich, W. Kataphinan, D. H. Reneker, P. Wang, Biotechnol. Prog., 2002, 18, 1027-1032.
[9] H. F. Jia, G. Y. Zhu, P. Wang, Biotechnol. Bioeng., 2003, 84, 406-414.
[10] M. B. F. Martins, S. I. D. Simoes, M. E. M. Cruz, R, J. Mater. Sci. Mater. Med., 1996, 7, 413-414.
[11] M. H. Liao, D. H. Chen, Biotechnol. Lett., 2001, 23, 1723-1727.
[12] S. H. Huang, M. H. Liao, D. H. Chen, Biotechnol. Prog., 2003, 19, 1095-1100.
[13] M. Koneracka, P. Kopcansky, M. Antalik, M. Timko, C. N. Ramchand, D. Lobo, R. V. Mehta, R. V. Upadhyay, J. Magn. Magn. Mater., 1999, 201, 427-430.
[14] A. Kondo, H. Fukuda, J. Ferment. Bioeng., 1997, 84, 337-341.
[15] C. M. Niemeyer, Angew. Chem. Int. Ed., 2001, 40, 4128-4158.
[16] A. Dyal, K. Loos, M. Noto, S. W. Chang, C. Spagnoli, K. V. P. M. Shafi, A. Ulman, M. Cowman, R. A. Gross, J. Am. Chem. Soc., 2003, 125, 1684-1685.
[17] S. Laurent, D. Forge, M. Port, A. Roch, C. Robic, L. V. Elst, R. N. Mul-ler, Chem. Rev., 2008, 108, 2064-2110.
[18] C. R. Lin, Y. M. Chu, S. C. Wang, Mater. Lett., 2006, 60, 447-450.
[19] B. Z. Zheng, M. H. Zhang, D. Xiao, Y. Jin, M. M. F. Choi, Inorg. Mater., 2010, 46, 1106-1111.
[20] A. Garcia III, S. Oh, C. R. Engler, Biotechnol. Bioeng., 1989, 33, 321-326.
[21] K. Selvam, M. Govarthanan, S. Kamala-Kannan, M. Govindharaju, B. Senthilkumar, T. Selvankumar, A. Sengottaiyan, RSC Adv., 2014, 4, 13045-13051.
[22] R. V. Mehta, R. V. Upadhyay, S. W. Charles, C. N. Ramchand, Bio-technol. Technol., 1997, 11, 493-496.
[23] M. L. Verma, R. Chaudhary, T. Tsuzuki, C. J. Barrow, M. Puri, Biore-source Technol., 2013, 135, 2-6.
[24] A. Kondo, T. Urabe, K. Higashitani, J. Fermant. Bioeng., 1994, 77, 700-703.
[25] O. H. Lowry, N. J. Roseborough, A. L. Farr, R. J. Rondall, J. Biol. Chem., 1951, 193, 265-275.
[26] J. N. Gao, X. Z. Ran, C. M. Shi, H. M. Cheng, T. M. Cheng, Y. P. Su, Nanoscale, 2013, 15, 7026-7033.
[27] J. S. Moon, K. K. Park, J. H. Kim, G. Seo, Appl. Catal. A, 2000, 201,81-89.
[28] J. Jordan, C. S. S. R. Kumar, C. Theegala, J. Mol. Catal. B, 2011, 68, 139-146.
[29] A. Ince, G. Bayramoglu, B. Karagoz, B. Altintas, N. Bicak, M. Y. Arica, Chem. Eng. J., 2012, 189-190, 404-412.
[30] T. L. Ogeda, I. B. Silva, L. C. Fidale, O. A. El Seoud, D. F. S. Petri, J. Biotechnol., 2012, 157, 246-252.
[31] Z. X. Tang, J. Q. Qian, L. E. Shi, Mater. Lett., 2007, 61, 37-40.
[32] G. K. Kouassi, J. Irudayaraj, G. McCarty, Biomagn. Res. Technol., 2005, 3, 1.
[33] S. M. Wang, P. Su, F. Y. Ding, Y. Yang, J. Mol. Catal. B, 2013, 89, 35-40.

Activity and stability of bacterial cellulase immobilized on magnetic nanoparticles

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