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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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Lineweaver-Burk plots for free and immobilized GOx at pH = 4 and pH = 7.
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f4-ijms-13-11870: Lineweaver-Burk plots for free and immobilized GOx at pH = 4 and pH = 7.

Mentions: The activities of the free and immobilized enzymes with various substrate concentrations were plotted as Lineweaver-Burk graphs to calculate Vmax and Km values (Figure 4, Table 3). The Vmax value defines the maximum velocity when all of the enzyme is saturated with substrate. Km, the substrate concentration at which an enzyme reaches ½ Vmax, reflects the effective characteristic of the enzyme and depends on both partitioning and diffusion [3].


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)

Lineweaver-Burk plots for free and immobilized GOx at pH = 4 and pH = 7.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f4-ijms-13-11870: Lineweaver-Burk plots for free and immobilized GOx at pH = 4 and pH = 7.
Mentions: The activities of the free and immobilized enzymes with various substrate concentrations were plotted as Lineweaver-Burk graphs to calculate Vmax and Km values (Figure 4, Table 3). The Vmax value defines the maximum velocity when all of the enzyme is saturated with substrate. Km, the substrate concentration at which an enzyme reaches ½ Vmax, reflects the effective characteristic of the enzyme and depends on both partitioning and diffusion [3].

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