Why Do Enzymes Increase Optimum Temperature
Enzymes are biological catalysts and each individual enzyme can only catalyse to one type of reaction – due to its specific shape. Each individual enzyme has its own specific shape which is determined by the amino acid sequence that it is made up of – each enzyme’s active site matches to its unique substrate molecule. For the sake of our experiment – enzymes catalyse reactions because they become an active site for reactions to take place. This lowers the energy that is needed for the reaction but at the same time, it increases the chance that they will happen. Enzymes have an optimum temperature range at which the reaction will work the best – in most cases the warmer the better. The reason behind this is because when particles become warmer,
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they move around faster because they have more energy – making the chances of collisions between an enzyme and its matching substrate higher. It’s important that these collisions happen because without them the substrate will never bond with the active site of an enzyme, meaning no reaction will take place. Although, if the temperature is increased beyond the optimum temperature range, the bonds in the enzyme then start to break, causing the shape of the active site of the enzyme to change.
If this happens, the substrate will no longer fit perfectly into the active site and they will not be able to bond to make the enzyme-substrate complex, resulting in no reaction taking place with the enzymes aid and instead the enzyme will denature. The opposite of this is when the temperature is too cold so the molecules have less energy, meaning they move around slower and the possibilities of collisions decrease. Less reactions happen at lower temperatures, which results in the hydrogen peroxide taking longer to break down. When doing our own experiment we saw this exact thing happen, and you can see this in our results. There is a clear difference between temperatures lower than 25ºC and higher than 55ºC, in the way the catalase broke down the hydrogen peroxide. From our results, it’s clear that these temperatures were enough to break the bonds in enzyme and then change the shape of the active site. Our results also show that the optimum temperature for the catalase was about 45ºC-55ºC – with the most energy to increase the amount of collisions but also not enough to change the shape of the active
site.
they move around faster because they have more energy – making the chances of collisions between an enzyme and its matching substrate higher. It’s important that these collisions happen because without them the substrate will never bond with the active site of an enzyme, meaning no reaction will take place. Although, if the temperature is increased beyond the optimum temperature range, the bonds in the enzyme then start to break, causing the shape of the active site of the enzyme to change.
If this happens, the substrate will no longer fit perfectly into the active site and they will not be able to bond to make the enzyme-substrate complex, resulting in no reaction taking place with the enzymes aid and instead the enzyme will denature. The opposite of this is when the temperature is too cold so the molecules have less energy, meaning they move around slower and the possibilities of collisions decrease. Less reactions happen at lower temperatures, which results in the hydrogen peroxide taking longer to break down. When doing our own experiment we saw this exact thing happen, and you can see this in our results. There is a clear difference between temperatures lower than 25ºC and higher than 55ºC, in the way the catalase broke down the hydrogen peroxide. From our results, it’s clear that these temperatures were enough to break the bonds in enzyme and then change the shape of the active site. Our results also show that the optimum temperature for the catalase was about 45ºC-55ºC – with the most energy to increase the amount of collisions but also not enough to change the shape of the active
site.