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Polystyrene attached Pt(IV)-azomethine, synthesis and immmobilization of glucose oxidase enzyme.

Sarı N, Antepli E, Nartop D, Yetim NK - Int J Mol Sci (2012)

Bottom Line: The characteristics of the immobilized glucose oxidase (APS-Sch-Pt-GOx) enzyme showed two optimum pH values that were pH = 4.0 and pH = 7.The insertion of stable Pt(IV)-azomethine spacers between the polystyrene backbone and the immobilized GOx, (APS-Sch-Pt-GOx), increases the enzymes' activity and improves their affinity towards the substrate even at pH = 4.The storage stability of the immobilized glucose oxidase was shown to be eleven months in dry conditions at +4 °C.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, Faculty of Science, Gazi University, Ankara 06500, Turkey; E-Mails: esinantpl@hotmail.com (E.A.); nurdankurnaz@gazi.edu.tr (N.K.Y.).

ABSTRACT
Modified polystyrene with Pt(IV)-azomethine (APS-Sch-Pt) was synthesized by means of condensation and demonstrated to be a promising enzyme support by studying the enzymatic properties of glucose oxidase enzyme (GOx) immobilized on it. The characteristics of the immobilized glucose oxidase (APS-Sch-Pt-GOx) enzyme showed two optimum pH values that were pH = 4.0 and pH = 7. The insertion of stable Pt(IV)-azomethine spacers between the polystyrene backbone and the immobilized GOx, (APS-Sch-Pt-GOx), increases the enzymes' activity and improves their affinity towards the substrate even at pH = 4. The influence of temperature, reusability and storage capacity on the free and immobilized glucose oxidase enzyme was investigated. The storage stability of the immobilized glucose oxidase was shown to be eleven months in dry conditions at +4 °C.

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Effect of pH on enzyme activity (a) and image of GOx–(APS–Sch–Pt) at optimum pH (b).
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f1-ijms-13-11870: Effect of pH on enzyme activity (a) and image of GOx–(APS–Sch–Pt) at optimum pH (b).

Mentions: The maximum activity was obtained at pH 5.0 for the free enzyme. Studying (APS–Sch–Pt), two maximum activities were observed at pH 4.0 and pH 7.0, which is different from earlier reports [14–16]. They are illustrated in Figure 1 and Table 2. As is known, pH is one of the important parameters capable of altering enzymatic activities in aqueous solution. Immobilization of the enzyme is likely to result in conformational changes of the enzyme resulting in a variation of the optimum pH. The reason for having two optima of immobilized (APS–Sch–Pt) may be due to the active properties of different residues of enzyme.


Polystyrene attached Pt(IV)-azomethine, synthesis and immmobilization of glucose oxidase enzyme.

Sarı N, Antepli E, Nartop D, Yetim NK - Int J Mol Sci (2012)

Effect of pH on enzyme activity (a) and image of GOx–(APS–Sch–Pt) at optimum pH (b).
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3472780&req=5

f1-ijms-13-11870: Effect of pH on enzyme activity (a) and image of GOx–(APS–Sch–Pt) at optimum pH (b).
Mentions: The maximum activity was obtained at pH 5.0 for the free enzyme. Studying (APS–Sch–Pt), two maximum activities were observed at pH 4.0 and pH 7.0, which is different from earlier reports [14–16]. They are illustrated in Figure 1 and Table 2. As is known, pH is one of the important parameters capable of altering enzymatic activities in aqueous solution. Immobilization of the enzyme is likely to result in conformational changes of the enzyme resulting in a variation of the optimum pH. The reason for having two optima of immobilized (APS–Sch–Pt) may be due to the active properties of different residues of enzyme.

Bottom Line: The characteristics of the immobilized glucose oxidase (APS-Sch-Pt-GOx) enzyme showed two optimum pH values that were pH = 4.0 and pH = 7.The insertion of stable Pt(IV)-azomethine spacers between the polystyrene backbone and the immobilized GOx, (APS-Sch-Pt-GOx), increases the enzymes' activity and improves their affinity towards the substrate even at pH = 4.The storage stability of the immobilized glucose oxidase was shown to be eleven months in dry conditions at +4 °C.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, Faculty of Science, Gazi University, Ankara 06500, Turkey; E-Mails: esinantpl@hotmail.com (E.A.); nurdankurnaz@gazi.edu.tr (N.K.Y.).

ABSTRACT
Modified polystyrene with Pt(IV)-azomethine (APS-Sch-Pt) was synthesized by means of condensation and demonstrated to be a promising enzyme support by studying the enzymatic properties of glucose oxidase enzyme (GOx) immobilized on it. The characteristics of the immobilized glucose oxidase (APS-Sch-Pt-GOx) enzyme showed two optimum pH values that were pH = 4.0 and pH = 7. The insertion of stable Pt(IV)-azomethine spacers between the polystyrene backbone and the immobilized GOx, (APS-Sch-Pt-GOx), increases the enzymes' activity and improves their affinity towards the substrate even at pH = 4. The influence of temperature, reusability and storage capacity on the free and immobilized glucose oxidase enzyme was investigated. The storage stability of the immobilized glucose oxidase was shown to be eleven months in dry conditions at +4 °C.

Show MeSH
Related in: MedlinePlus