The effect of enzyme and substrate concentration on a reaction rate
Effect of substrate concentration on enzyme activity lab report
This increases the chances of a successful collision and so the rate increases. Immobilized enzymes Enzymes are widely used commercially, for example in the detergent, food and brewing industries. Research question Investigation on the effect of different substrate concentrations, which in this case are the manipulated hydrogen peroxide concentrations on the rate of enzyme activity of catalase in liver on the decomposition of the hydrogen peroxide. A number of ways of re-arranging the Michaelis-Menten equation have been devised to obtain linear relationships which permit more precise fitting to the experimental points, and estimation of the values of Km and Vmax. Hypothesis The hypothesis of this practical is that the rate of reaction will indeed increase with the increase of hydrogen peroxide concentrations, only if the other crucial factors of enzyme activity are kept constant, such as pH, enzyme concentration, inhibition and temperature. What is most likely to happen to the activity of the enzyme if the pH increases to 8. If it is the limiting factor, increasing concentration will increase the rate of reaction up to a point, after which any increase will not affect the rate of reaction. At this point, so much substrate is present that essentially all of the enzyme active sites have substrate bound to them. An example would be the magnesium ions that interact with ATP or other negatively charged nucleotides, thus decreasing their overall charge making the binding of them to the active site more efficient and higher velocity in the enzymatic reaction. The change in shape is 'induced' by the approaching substrate molecule. Concentration of enzyme and substrate The rate of an enzyme-catalysed reaction depends on the concentrations of enzyme and substrate. However, the effect of bond breaking will become greater and greater, and the rate of reaction will begin to decrease. The reason to why the soap is used in this practical, it to be able to measure the gas made from the reaction, which can otherwise not be seen without the foam obtaining it. This is because changes in pH can make and break intra- and intermolecular bonds, changing the shape of the enzyme and, therefore, its effectiveness.
Different enzymes have different Optimum pH values. How enzymes lower the activation energy, is by holding the molecules packet together increasing the chance of a reaction to occur and thus lowering the activation energy. There is a certain temperature at which an enzyme's catalytic activity is at its greatest see graph.
In summary, as temperature increases, initially the rate of reaction will increase, because of increased Kinetic Energy. In enzyme reactions, a substrate binds to the active site on the enzyme, forming an enzyme-substrate complex where the enzyme breaks down the bonds in the substrate, creating a whole new bond and formation which will lead to the product and during and after the whole process the enzyme will remain unchanged, thus being able to react in other chemical reactions again.
This optimal temperature is usually around human body temperature Additionally, the reaction rate depends on properties of the enzyme K, kcat and the enzyme concentration E.
Effect of enzyme concentration on enzyme activity experiment
The rate would simply be higher 20 or 30 people in 10 minutes before it leveled off. This interference causes a change in shape of the enzyme, and importantly, its Active Site. Hypothesis The hypothesis of this practical is that the rate of reaction will indeed increase with the increase of hydrogen peroxide concentrations, only if the other crucial factors of enzyme activity are kept constant, such as pH, enzyme concentration, inhibition and temperature. Controlling these factors in a cell is one way that an organism regulates its enzyme activity and so its Metabolism. Skip the theory and go straight to: How to determine Km and Vmax A simple chemical reaction with a single substrate shows a linear relationship between the rate of formation of product and the concentration of substrate, as shown below: For an enzyme-catalysed reaction, there is usually a hyperbolic relationship between the rate of reaction and the concentration of substrate, as shown below: A At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration. The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction, Vmax. Eventually, the enzyme will become Denatured and will no longer function. This optimal temperature is usually around human body temperature B As the concentration of substrate increases, the enzyme becomes saturated with substrate. An enzyme with a high Km has a low affinity for its substrate, and requires a greater concentration of substrate to achieve Vmax. Concept Review Exercises The concentration of substrate X is low.
If only 5 people are present at the stand, the rate of their arrival at the concert hall is 5 people in 10 minutes.
based on 5 review