Influence of load on the recycling stability of nanospheres attached platinium ion for determination of glucose

Elvan Hasanoglu Ozkan; Nursen Sarı; Dilek Nartop; Nurdan Kurnaz Yetim

Journal of Industrial and Engineering Chemistry, Vol.25, 180-185, May, 2015

DOI10.1016/j.jiec.2014.10.031 Export Citation

Influence of load on the recycling stability of nanospheres attached platinium ion for determination of glucose

Elvan Hasanoglu Ozkan¹, Nursen Sarı^{1, †}, Dilek Nartop², and Nurdan Kurnaz Yetim^{1, 3}

¹Department of Chemistry, Faculty of Science, Gazi University, Teknikokullar, Ankara 06500, Turkiye, Turkey
²Department of Chemistry, Faculty of Arts and Science, Nevsehir University, 2000 Evler Mh. Zubeyde Hanım Cd, Nevs¸ ehir 50300, Turkiye, Turkey
³Department of Chemistry, Faculty of Sciences and Art, Kırklareli University, Kırklareli, Turkiye, Turkey

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New nanospheres have been prepared with Pt2+ and Pt4+ for compare enzymatic properties of glucose oxidase enzyme (GOx). In this study nanoparticles, (aminomethyl)polystyrene (APS), 2-hydroxy-5-methylbenzaldehyde and Pt2+/Pt4+ have been synthesized by means of template and investigated the enzymatic properties of glucose oxidase enzyme (GOx) immobilized on there. The characteristics of the immobilized glucose oxidase (APS?Pt2+?GOx and APS-Pt4+-GOx) enzyme showed one optimum pH value. The influence of temperature, reusability and storage capacity on the free and immobilized glucose oxidase enzyme have been investigated. It is found that nanosphere including platinium atom exhibits excellent performance as the immobilized supporter of GOx, the immobilized enzyme demonstrates perfected storage and recycling stability. APS-Pt2+-GOx retains more than 30% of the initial activity after 32 successive cycles, which is a remarkable result.

Keywords:Biocatalysis;Glucose oxidase;Nanospheres;Platinium ion

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[Referenced By]

[1] Zhang Y, Chen Y, Zhang H, Zhang B, Liu J, J. Inorg. Biochem., 118, 59 (2013)

[2] Shenhar R, Norsten TB, Rotello VM, Adv. Mater., 17(6), 657 (2005)

[3] De Jong WH, Borm PJA, Int. J. Nanomed., 3(2), 133 (2008)

[4] Toshima N, Yonezawa T, New J. Chem., 22, 1179 (1998)

[5] Colak O, Yasar A, Cete S, Arslan F, Artif. Cells Blood Substit. Biotechnol, 40, 354 (2012)

[6] Juan L, Xingzhang Q, Zhanjun Y, Huamei Q, Qin X, Guowang D, Talanta, 104, 116 (2013)

[7] Yen MY, Tng CC, Hsiao MC, Liu PI, Chuang WP, Ma CCM, Hsieh CK, Tsai MC, Tsai CH, J. Mater. Chem., 21, 12880 (2011)

[8] Aynacı E, Sarı N, Tumturk H, Artiff, Cells Blood Substitutes, 39, 259 (2011)

[9] Erduran V, Tumturk H, Aynacı E, Sarı N, J. Macromol. Sci., 50, 871 (2013)

[10] Singh V, Singh D, Ind. Eng. Chem. Res., 53(10), 3854 (2014)

[11] Arslan F, Ustabas S, Arslan H, Sensors, 11, 8152 (2011)

[12] Liu Y, Yuan M, Qiao L, Guo R, Biosens. Bioelectron., 52, 391 (2014)

[13] Huang J, Zhao R, Wang H, Zhao WQ, Ding LY, Biotechnol. Lett., 32(6), 817 (2010)

[14] Ge J, Lu D, Liu Z, Lui Z, Biochem. Eng. J., 44, 53 (2009)

[15] Xie JB, Hsieh YL, J. Mater. Sci., 38(10), 2125 (2003)

[16] Ren GL, Xu XH, Liu Q, Cheng J, Yuan XY, Wu LL, Wan YZ, React. Funct. Polym., 66(12), 1559 (2006)

[17] Guisan JM 2nd, Immobilization of Enzymes and Cells, Humana Press Inc., Totowa, NJ, 2006 p. 14.

[18] Trinder P, Ann. Clin. Biochem., 6, 24 (1969)

[19] Arslan H, Ozdemir M, Zengin H, Int. J. Electrochem. Sci., 7, 10205 (2012)

[20] Sarı N, Ozcan S, Chin. J. Polym. Sci., 27, 675 (2009)

[21] Sar1 N, Yuzuak N, J. Inorg. Organomet. Polym., 16, 259 (2006)

[22] Sar1 N, Antepli E, Nartop D, Yetim NK, Int. J. Mol. Sci., 13, 11870 (2012)

[23] Wang X, Zhu KX, Zhou HM, Int. J. Mol. Sci., 12(5), 3042 (2011)

[24] Pazur JH, Kleppe K, Cepure A, Arch. Biochem. Biophys., 111, 351 (1965)