Hydrogen Ions Lab

We increased the substrate, catechol, while maintaining the enzyme, catecholase, at the same volume. We came to the hypothesis that if the substrate was increased, then the rate of reaction would increase as long as there is enzymes to react with. The third experiment involved how temperature would affect enzyme activity. This was done by placing certain vials in certain temperatures and then analyzing the data in the spectrophotometer. We came to the hypothesis that if the temperature was increased, then the reaction rate would increase until it reaches the optimal temperature after that the reaction rate would decrease. This is because the enzyme will start to denature if the temperatures get too high or too low. The fourth experiment deals with how pH affects enzyme activity. For this experiment different vials with catecholase and different pH’s were observed under a spectrophotometer to see how the enzyme would be affected. We found our hypothesis to be, if pH is raised, then the reaction rate will increase until it reaches the optimal pH. The reaction rate will increase until the optimal pH because after the optimal pH, the enzyme will start to denature and not function as it

As stated in the introduction, three conditions that may affect enzyme activity are salinity, temperature, and pH. In experiment two, we explored how temperature can affect enzymatic activity. Since most enzymes function best at their optimum temperature or room temperature, it was expected that the best reaction is in this environment. The higher the temperature that faster the reaction unless the enzyme is denatured because it is too hot. Similarly, pH and salinity can affect enzyme activity.

INTRODUCTION: Enzymes are catalysts that speed up reactions by lowering activation energy. Activation energy is the amount of energy needed for a reaction to take place. Enzymes act on substrates which bind to the enzymes’ active site. The enzyme changes its shape to accommodate the substrate which creates the new product. Furthermore, there are optimal conditions which will allow the enzymes to function at its highest rate. These opyimal conditions include temperature, pH levels, and the concentration of the enzyme (Fox, 2013). If the environment is not suited for the enzymes’ optimal conditions then enzymatic reactions cannot occur at its highest rate or may not even react at all. For example, if the temperature is higher than the enzyme’s optimal temperature then the enzyme may become denatured.

The pH of the surrounding solution can alter the binding site on the enzyme, change the structure of the protein truture of enzyme, and alter the ionization station of the enzyme or substrate. However, in this experiment, it tested the rationship between the substrate soncentration and the reaction rate. The lab results are suppoting the hypothesis that the higher the substrate concentration is the higher the reaction rate is. The deffenence in balloon circumference is 7cm when the stubstrate concentration is 3%; the difference in balloon circumference is 3.5cm when the stubstrate concentration is 1.5%; the difference in balloon circumference is 0.5cm when the stubstrate concentration is 0.75%, and the difference in balloon is 0cm when the stubstrate concentration is 0%. Nonetheless, this lab did not discuess the maximum

The motive of this lab is to attain a better understanding of enzyme activity by timing chemical reactions in certain temperatures and pH levels. Enzymes act as catalysts that help speed up reactions. Without these enzymes chemical reactions in metabolism would be backed up. There are two factors that affect an enzyme’s reaction rate: temperature and pH levels. In this label we will be testing different pH levels and temperatures to see which ones cause the most reactions.

Substrate concentration also affects the rate of reaction as the greater the substrate concentration the faster the rate of reaction and all the active sites are filled. At this point the rate of reaction can only be increased if you add more enzymes in to make more active sites available.

1. pH. Amino acid side chains contain groups such as - COOH and NH2 that readily gain or lose H+ ions. As the pH is lowered an enzyme will tend to gain H+ ions, and eventually enough side chains will be affected so the enzyme's shape is disrupted. Likewise, as the pH is raised, the enzymes will lose H+ ions and eventually lose its active shape. Many of the enzymes function properly in the neutral pH range and are denatured at either an extremely high or low pH. Some

The Effect of low pH on Enzyme Activity Frank Keith Welsh, BIO 102, Fall semester Today I will be providing an experiment on the effects of pH on enzymes. Enzymes are affected by changes in pH. Exceptionally high or low pH values commonly cause in complete loss of activity for most enzymes. Furthermore to include temperature and pH there are other elements, such as ionic strength, that can shake the enzymatic reaction. To each of these both physical and chemical parameters should be considered and optimized for an enzymatic reaction to be precise.

The purpose of this report is to determine which catalyst effect the rate of enzyme activity within a experiment. Enzymes lower the energy of activation by binding with substrate in chemical reactions to allow the reaction to occur. energy activation is the reguired amount of energy required amount of energy needed to start a chemical reaction. This decreases the faster the enzyme reaction goes by the shape change on an active site. the conclusion is that the enviromental conditions such as pH, temperature help speed up the reaction rate but also the amount of substrate concentration and the abosrbance over time all affect the amount of enzyme activity.

How does an enzyme affect reaction rates, and how does the acid affect the enzyme itself? In this most recent catalase lab, data both conclusive and inconclusive answered these questions. In the data collected, the major trend was when the hydrogen peroxide concentration (independent variable) increased, the reaction time (dependent variable) of the enzyme decreased. One of the data points did not follow this trend, and will be addressed later. Also, when the acid was added to the enzyme, the reaction still took place, rendering our data inconclusive. When a paper disk was taken out of the catalase for the first time, it was placed in 100% hydrogen peroxide, which reared quick results. The paper rose in 23.37 seconds, but for the majority of

It decreases the activation energy in reaction. When the substrate binds to the active site on enzyme, it will change the conformation of enzyme to make the enzyme-substrate complex and catalyze reactions2. The reason we want to analyze enzyme kinetic in order to quantitative biocatalysis, understand the catalytic mechanism and understand regulation of

Denaturation is where the proteins of an enzyme unfold and the structure of an enzyme irreversibly changes so that it cannot perform its intended function. An example of non-specific enzyme inhibitors would be temperature and pH. If the conditions are too acidic or too alkaline, or the temperature is too high, the structure of the enzyme will denature. If the active site of an enzyme is altered, then the substrate cannot fit in to the enzyme and the chemical reaction will not take place.

= PH changes affect the structure of an enzyme molecule and therefore affect its ability to bind with its substrate molecules. Changes in pH affect the ionic bonds and hydrogen bonds that hold the enzyme together, which naturally affects the rate of reaction of the enzyme with the substrate. On top if this, the hydrogen ions neutralise the negative charges of the R groups in the

The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the

The concentration of enzymes and substrates affects the rate of reaction, as the concentration of the enzyme and substrate is increased, the velocity of the reaction proportionately increases. By increasing the concentration of substrate it will gradually increase the velocity of enzyme reaction within the restricted range of substrate levels.