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A metabolic pathway in yeast using immobilisation

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Introduction

A metabolic pathway in yeast using immobilisation Conclusion As you can see from my graph there is a basic trend. This is that as the carbon dioxide increases with time the rate of reaction increases for the yeast. The volume of carbon dioxide increases because the yeast is respiring anaerobically; the yeast breaks down the glucose and produces carbon dioxide and alcohol as a waste product. This process is fermentation. The equation for this reaction is: Oxygen + Glucose Ethanol + Carbon dioxide + Energy (O2) (C6H12O6) (C2H5OH) (CO2) The carbon dioxide is produced because the substrate (sucrose solution) binds to the active site of the enzyme (free yeast). ...read more.

Middle

Immobilised enzymes have slower rate of reaction than non- immobilised enzymes (free enzymes). This is shown on the graph at 10 minutes. The yeast has a gradient of 0.45 and the beads have a gradient of 0.14. This is because alcohol is produced from fermentation. Ethanol is the alcohol produced, which eventually accumulates and kills the yeast. The substrate (glucose solution) binds into the active site of the enzyme forming an enzyme-substrate complex. The enzyme-substrate complex breaks down to give the product carbon dioxide and alcohol. The alcohol is the end product inhibitor of a metabolic pathway, which begins to accumulate. The alcohol acts as a non-competitive inhibitor and binds with the enzyme at a site other than the active site. ...read more.

Conclusion

Therefor the rate of reaction increases. The immobilised enzymes have a smaller surface area so there is a less chance of the substrate binding with the active site. This produces less enzyme-substrate complex; therefor the rate of reaction is lower. As you can see from my graph both of the curves do not finish at the same place, if I carried on with my experiment eventually the curves would finish at the same place. This is because at T14 for the yeast (value: 14.7) and beads (Value: 12.1) there is a high concentration of substrate, this produces lots enzyme-substrate complex, so the rate of reaction increases. Eventually there will be less substrates then enzymes because more products have been formed. When there are no substrates, there are no enzyme-substrate complex so the rate of reaction is zero. ...read more.

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