A metabolic pathway in yeast using immobilisation
- Words:
- 639
- Submitted:
- Thu Sep 04 2003

Have a little read: ... 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). The active site is an area of an enzyme, which the substrate fits in order to catalyse a reaction to which carbon dioxide and alcohol is produced. Immobilised enzymes are enzymes bounded immovably to a surface and not allowed to dissolve in a solution. Also looking at my graph there is a pattern, this is that as the carbon dioxide increases with time the rate of reaction increases for the beads. The beads are immobilised enzymes. The rate of reaction increases because the enzyme (immobilised enzymes) and the substrate (glucose solution) have kinetic energy to move. The more energy they have the more number of collisions. Therefore there is a greater chance of the substrate binding into the active site of the enzyme. This produces an enzyme - substrate complex, this then breaks down to give carbon dioxide and alcohol. 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. This changes the shape of the structure of the active site. Therefore the rate of reaction decreases. As the carbon dioxide concentration builds up in the beads the beads will start to rise to the surface, this
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