Figures & data
Figure 1 Current difference-concentration curves obtained for the electrooxidation of H2O2 at Pt, PVF+ClO4− modified and enzyme electrodes: ▪: Pt, ▴: PVF+ClO4− modified, ♦: creatine enzyme electrodes (0.05M pH 7.5 phosphate buffer, 25°C).
![Figure 1 Current difference-concentration curves obtained for the electrooxidation of H2O2 at Pt, PVF+ClO4− modified and enzyme electrodes: ▪: Pt, ▴: PVF+ClO4− modified, ♦: creatine enzyme electrodes (0.05M pH 7.5 phosphate buffer, 25°C).](/cms/asset/3b0e35b4-d730-4b3c-a1fc-d7f7bfc459b2/ianb19_a_158160_f0001_b.gif)
Figure 2 Creatine response of the enzyme electrodes, İmmobilization method; ♦: Adsorption ▪: Immersing into GA ▴: Crosslinking with GA-BSA (0.05 M pH 7.5 phosphate buffer, 25°C).
![Figure 2 Creatine response of the enzyme electrodes, İmmobilization method; ♦: Adsorption ▪: Immersing into GA ▴: Crosslinking with GA-BSA (0.05 M pH 7.5 phosphate buffer, 25°C).](/cms/asset/db739306-139b-4682-988f-b81432505a97/ianb19_a_158160_f0002_b.gif)
Figure 3 The reproducibility of the enzyme electrode (Immobilization method: adsorption; 0.05 M pH 7.5 phosphate buffer, 25°C).
![Figure 3 The reproducibility of the enzyme electrode (Immobilization method: adsorption; 0.05 M pH 7.5 phosphate buffer, 25°C).](/cms/asset/83cf6ac3-6eef-4973-bd75-2ecfabd84e27/ianb19_a_158160_f0003_b.gif)
Figure 4 The reproducibility of the enzyme electrode prepared by immersing into GA (0.05 M pH 7.5 phosphate buffer, 25°C).
![Figure 4 The reproducibility of the enzyme electrode prepared by immersing into GA (0.05 M pH 7.5 phosphate buffer, 25°C).](/cms/asset/024d4ba6-4fc5-468b-a1c0-44218cba4003/ianb19_a_158160_f0004_b.gif)
Figure 5 The effect of the solution (1.4 × 10−5 M creatine) pH on the response of the electrode in 0.05 M phosphate buffer solution at 25°C.
![Figure 5 The effect of the solution (1.4 × 10−5 M creatine) pH on the response of the electrode in 0.05 M phosphate buffer solution at 25°C.](/cms/asset/3ebb63de-637f-43b1-96cf-8f738d1a98d3/ianb19_a_158160_f0005_b.gif)
Figure 6 The effect of temperature on the response of enzyme electrode against creatine (0.05 M pH 7.5 phosphate buffer).
![Figure 6 The effect of temperature on the response of enzyme electrode against creatine (0.05 M pH 7.5 phosphate buffer).](/cms/asset/ba3b8c6f-97c0-43c2-898f-e43aea695fcc/ianb19_a_158160_f0006_b.gif)
Figure 7 The effect of the phosphate concentration on the response of the enzyme electrode against creatine (pH 7.5 phosphate buffer, 25°C).
![Figure 7 The effect of the phosphate concentration on the response of the enzyme electrode against creatine (pH 7.5 phosphate buffer, 25°C).](/cms/asset/594b7eba-d5ed-4766-bd42-3dc806dbbea0/ianb19_a_158160_f0007_b.gif)
Figure 8 The effect of enzyme ratio on the response of enzyme electrode against creatine (0.05 M pH 7.5 phosphate buffer, 25°C).
![Figure 8 The effect of enzyme ratio on the response of enzyme electrode against creatine (0.05 M pH 7.5 phosphate buffer, 25°C).](/cms/asset/66e8f585-b91d-4127-aa82-a1f10d0fdec5/ianb19_a_158160_f0008_b.gif)
Figure 9 The reproducibility of the electrode prepared by crosslinking with GA-BSA system (0.05 M pH 7.5 phosphate buffer, 25°C).
![Figure 9 The reproducibility of the electrode prepared by crosslinking with GA-BSA system (0.05 M pH 7.5 phosphate buffer, 25°C).](/cms/asset/4071c3f6-5575-42b9-b62d-c6907f40b715/ianb19_a_158160_f0009_b.gif)
Figure 10 Storage stabilization of the enzyme electrode prepared by crosslinking with GA-BSA system (0.05 M pH 7.5 phosphate buffer, 4°C).
![Figure 10 Storage stabilization of the enzyme electrode prepared by crosslinking with GA-BSA system (0.05 M pH 7.5 phosphate buffer, 4°C).](/cms/asset/623af444-2a2e-40c9-a881-b45418ae39ef/ianb19_a_158160_f0010_b.gif)
Table 1 The properties and the optimum working conditions of the enzyme electrode