Glucose Oxidase Immobilization on TMAH-Modified Bentonite

https://doi.org/10.22146/ijc.21219

Ruth Chrisnasari(1*), Zerlina Gabriela Wuisan(2), Arief Budhyantoro(3), Restu Kartiko Widi(4)

(1) Department of Biology, Faculty of Biotechnology, University of Surabaya, FG Building 2nd floor, Jl. Raya Kalirungkut Surabaya 60293
(2) Department of Biology, Faculty of Biotechnology, University of Surabaya, FG Building 2nd floor, Jl. Raya Kalirungkut Surabaya 60293
(3) Department of Chemical Engineering, Faculty of Engineering, University of Surabaya, TG Building 6th floor, Jl. Raya Kalirungkut Surabaya 60293
(4) Department of Chemical Engineering, Faculty of Engineering, University of Surabaya, TG Building 6th floor, Jl. Raya Kalirungkut Surabaya 60293
(*) Corresponding Author

Abstract


The influence of bentonite modification by tetramethyl ammonium hydroxide (TMAH) on its capability to immobilize glucose oxidase (GOX) was studied. Modification of bentonite was conducted by the adding of 0-5% (v/v) TMAH. The observed results show that the different concentrations of TMAH affect the percentage of immobilized enzyme. The results of this study show that the best concentration of TMAH is 5% (v/v) which can immobilize up to 84.71% of GOX. X-ray diffraction (XRD) and Fourier Transforms Infrared Spectroscopy (FTIR) studies have been carried out to observe the structural changes in bentonite due to TMAH modification. The obtained immobilized GOX show the optimum catalytic activity on reaction temperature of 40-50 °C and pH of 7. The immobilized GOX kinetics at the optimum conditions determined the Km and Vmax value to be 4.96x10-2 mM and 4.99x10-3 mM.min-1 respectively. In addition, the immobilized GOX on TMAH-modified bentonite is stable enough so it could be re-used six times before its activity decreased by 39.44%.

Keywords


Tetramethyl Ammonium Hydroxide (TMAH); bentonite; immobilization; glucose oxidase

Full Text:

Full Text Pdf


References

[1] Sakizci, M., Alver, B.E., Alver, Ö., and Yörükoğullari, E, 2010, J. Mol. Struct., 969(1-2), 187–191.

[2] Peng, X., Luan, Z., Chen, F., Tian, B., and Jia, Z., 2005, Desalination, 174(2), 135–143.

[3] Dong, H., Li, J., Li, Y., Hu, L., and Luo, D., 2012, Chem. Eng. J., 181-82, 590–596.

[4] Smith, J.A., and Galan, A., 1995, Environ. Sci. Technol., 29(3), 685–692.

[5] Anirudhan, T.S., Suchithra, P.S., and Rijith, S., 2008, Colloids Surf., A, 326(3),147–156.

[6] Zhaoa, G., Zhang, H., Fan, Q., Ren, X., Li, J., Chen, Y., Wang, X., and Chao, H.P., 2010, J. Hazard. Mater, 173(1-3), 661–668.

[7] Li, Q., Su, Y., Yue, Q-Y., and Gao, B-Y., 2011, Appl. Clay Sci., 53(4), 760–765.

[8] Öztürk, N., Tabak, A., Akgöl, S., Uzun, L., and Denizli, A., 2007, J. Biol. Chem., 35 (1), 67-76.

[9] Öztürk, N., Tabak, A., Akgöl, S., and Denizli, A., 2007, Colloids Surf., A, 301, 490–497.

[10] Didi, M.A., Makhoukhi, B., Azzouz, A., and Villemin, D., 2009, Appl. Clay Sci., 42(3-4), 336–344.

[11] Yeşiloğlu, Y., 2005, Proc. Biochem., 40(6), 2155–2159.

[12] Ghiaci, M., Aghaei, H., Soleimanian, S., and Sedaghat, M.E., 2009, Appl. Clay Sci., 43(3-4), 289–295.

[13] Ghiaci, M., Aghaei, H., Soleimanian, S., and Sedaghat, M.E., 2009, Appl. Clay Sci., 43(3-4), 308–316.

[14] Cengiz, S., Çavaş, L., and Yurdakoç, K., 2012, Appl. Clay Sci., 65-66, 114–120.

[15] Vroemen, A.J., 2003, Handbook of Food Enzymology, Marcel Dekker, Inc, New York, 425–432.

[16] Wang, C-C., Juang, L-C., Lee, C-K., Hsu, T-C., Lee, J-F., and Chao, H-P., 2004, J. Colloid Interface Sci., 280(1), 27–35.

[17] Majdan, M., Sabah, E., Bujacka, M., Pikus, S., and Płaska, A.G., 2009, J. Mol. Struct., 938(1-3), 29–34.

[18] Sedaghat, M.E., Ghiaci, M., Aghaei, H., and Soleimanian-Zad, S., 2009, Appl. Clay Sci., 46(2), 125–130.

[19] Whittington, H., Kerry-Williams, S., Bidgood, K., Dodsworth, N., Peberdy, J., Dobson, M., Hincliffe, E., and Balance, D.J., 1990, Curr. Genet., 18(6), 531–536.

[20] Hartree, E.F., 1972, Anal. Biochem., 48(2), 422–427.

[21] Shuler, M., Kargi, F., 2002, Bioprocess Engineering: Basic Concepts, 2nd ed. Prentice-Hall, Upper Sadle River, NJ.

[22] Rauf, S., Ihsan, A., Akhtar, K., Ghauri, M.A., Rahman, M., Anwar, M.A., and Khalid, A.M., 2006, J. Biotechnol., 121(3), 351–360.



DOI: https://doi.org/10.22146/ijc.21219

Article Metrics

Abstract views : 3422 | views : 2404


Copyright (c) 2015 Indonesian Journal of Chemistry

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

 

Indonesian Journal of Chemistry (ISSN 1411-9420 /e-ISSN 2460-1578) - Chemistry Department, Universitas Gadjah Mada, Indonesia.

Web Analytics View The Statistics of Indones. J. Chem.