Hydrogen Peroxide Investigation

Investigation of hydrogen peroxide When hydrogen peroxide is added to fresh potatoes, bubbles form. Using a larger potato piece produces more bubbles. A possible explanation for this observation can be the evolution of oxygen when hydrogen peroxide is decomposed by enzyme catalase. Most potatoes contain a relatively small amount of high catalase, so a large amount of oxygen is produced.

In my lecture, I will study the reaction of potato enzyme with hydrogen peroxide. In particular, investigate the influence of the change in surface area of ​​potatoes when adding hydrogen peroxide. This is because as the surface area of ​​the potatoes increases, the reaction rate increases as the particles from potato and hydrogen peroxide collide more surface area and the larger the surface area, the more particles carry kinetic energy . By carrying more kinetic energy, the reaction is more likely to achieve its activation energy, thus creating a more successful collision and increasing the rate of reaction through a more successful collision.

Esthe.com/ investigated the effect of increased potato surface area when mixed with hydrogen peroxide

The effect of increasing the surface area of ​​the potatoes after mixing with hydrogen peroxide was studied.

Investigation of hydrogen peroxide When hydrogen peroxide is added to fresh potatoes, bubbles form. Using a larger potato piece produces more bubbles. A possible explanation for this observation can be the evolution of oxygen when hydrogen peroxide is decomposed by enzyme catalase.

Catalase concentration and catalase degradation rate AIM knows whether the concentration of hydrogen peroxide affects the decomposition rate of hydrogen peroxide by catalase decomposition. Scientific Knowledge Hydrogen peroxide is a byproduct of many chemical reactions in organisms. It is toxic and must therefore be degraded by the enzyme catalase found in most organisms. For example. Hydrogen Peroxide Catalase Water + Oxygen 2 H 2 O 2 (aq) 2 H 2 O + O 2 Enzyme Catalase (peroxidase) is the first enzyme found and is one of the fastest enzymes,

Catalase and peroxidase are heme enzymes that catalyze the reaction of hydrogen peroxide. In the case of 94, 95 catalase, the enzyme reaction is a disproportionation reaction of hydrogen peroxide (reaction 5.82). It seems that its function is to prevent the accumulation of potentially dangerous oxidizing agent. (For molecular oxygen toxicity, see Section III). The X-ray crystal structure of horseradish peroxidase 80 and the high spin iron state of dormancy of horseradish peroxidase 96 have been determined. In both cases, the active site has a hemoglobin b group. In catalase, the axial ligand is a phenolate derived from a tyrosyl residue that binds hemoglobin on the side remote from the active site cavity, water can bind to heme and catalyze in the cavity. The reaction is replaced by hydrogen peroxide. In horseradish peroxidase, the axial ligand is imidazole derived from histidyl residues.