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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 temperature on enzyme activity and image of GOx–(APS–Sch–Pt) (a) and free-GOx at optimum temperature (b).
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f2-ijms-13-11870: Effect of temperature on enzyme activity and image of GOx–(APS–Sch–Pt) (a) and free-GOx at optimum temperature (b).

Mentions: The effect of temperature on the activity of free and immobilized glucose oxidase is shown in Figure 2. There is a significant difference between the profiles of the temperature optimum for free and immobilized GOx. The optimum temperature for free GOx in pH = 4 is not shown due to denatured (Figure 2b). But, surprisingly, the optimum temperature for immobilized glucose oxidase was found to be 40 °C at pH = 4. Also, at pH = 7, the free and immobilized enzyme activities depended on temperatures in a range of 20 °C–90 °C, indicating that the optimal temperature for attaining the highest activities of free and immobilized GOx was 60 °C and 70 °C, respectively (Table 2). The results show that the immobilized enzyme, especially in a coordination covalently bound system, becomes more stable against heat and denaturing agents.


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

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

f2-ijms-13-11870: Effect of temperature on enzyme activity and image of GOx–(APS–Sch–Pt) (a) and free-GOx at optimum temperature (b).
Mentions: The effect of temperature on the activity of free and immobilized glucose oxidase is shown in Figure 2. There is a significant difference between the profiles of the temperature optimum for free and immobilized GOx. The optimum temperature for free GOx in pH = 4 is not shown due to denatured (Figure 2b). But, surprisingly, the optimum temperature for immobilized glucose oxidase was found to be 40 °C at pH = 4. Also, at pH = 7, the free and immobilized enzyme activities depended on temperatures in a range of 20 °C–90 °C, indicating that the optimal temperature for attaining the highest activities of free and immobilized GOx was 60 °C and 70 °C, respectively (Table 2). The results show that the immobilized enzyme, especially in a coordination covalently bound system, becomes more stable against heat and denaturing agents.

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