Wait a second!
More handpicked essays just for you.
More handpicked essays just for you.
Ph activity on enzyme activity
The effect of changing temperature on enzyme activity
Investigation of enzymes
Don’t take our word for it - see why 10 million students trust us with their essay needs.
Recommended: Ph activity on enzyme activity
Discussion/Analysis 1. If gas bubbles form then fermentation occurred. Glucose. Carbon dioxide. The enzyme didn’t recognize the structure of glactose, because of the orientation of the H and OH on the carbon 4 is different than glucose. The enzyme only identifies very specific substances. 2. In order to determine how fast a reaction is occurring there must be a basis for measurement. There must also be an indicator substances to determine the change that took place. Then there must be a tool to measure the change. In this lab a spectrophotometer was used. The ABS value is the actual value and it is used to determine the rate of change. 3. The higher the concentration of the enzyme the more there are to catalyze the reaction. Taking information from graph 1 (change in mL of enzyme), the more mL of enzymes that there are the faster the reaction rate is. It would increase until there was no substrate left available for a reaction. 4. At 5’C the reaction was slow because molecule movement gets slower when the temperature is lowered. The enzyme was broken down after it was exposed to 100’c and was unable to catalyze a reaction. At room temperature the reaction was the best, because it was not too cold and not too hot. 5. Decreasing or increasing the pH slowed the rate of reaction. The pH of 7 was the best for the reaction. If there are more H or more OH in the solution then the reaction is inhibited, because they disrupt the active site. 6. The inhibitor slowed and almost stopped the reaction rate. The inhibitor was able to bind to the enzymes active site and made it hard for it to catalyze a reaction with peroxide. Introduction Molecules called enzymes help catalyze reactions. A substrate is the molecule on which the enzyme acts. Most enzymes are proteins that have grooves in them called active sites that recognizes the substrate.
Enzymes are biomolecules that catalyze or assist chemical reactions. ("Enzyme Information - Disabled World", n.d.,) Without enzymes it would be impossible for an organism to carry out chemical reactions. Enzymes are proteins that carry a chemical reaction for a specific substance or nutrient. For example, the digestive enzymes help food to be broken down so it can be absorbed. Enzymes can either initiate the reaction or speed it up. Substrates are the chemicals that are transformed by enzymes. (Gunsch & Foster, 2014) Reactants are the chemicals in the absence of enzymes. Metabolic pathways that occur in a cell are determined by a set of enzymes which are selective for their substrates and catalyze only a few reactions among the many possibilities.
Investigating the Activity of an Enzyme Sucrose using the enzyme sucrase (invertase) can be broken down into. Glucose and Fructose -. The aim of this experiment was to find out about the activity of enzymes through measuring the micromoles of sucrase. expressed whilst the following reaction occurs:-. SUCRASE [ IMAGE ] SUCROSE GLUCOSE + FRUCTOSE C12H2201 H20 C6H12O6 C6H12O6
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
When molecules bump into each other, the kinetic energy that they have can be converted into chemical potential energy of the molecules. If the potential energy of the molecule becomes great enough, the activation energy of a reaction can be archived and a change in chemical state will result. Thus the greater the kinetic energy of the molecules in a system, the greater the resulting chemical potential energy. As the temperature of a system is increased it is possible that more molecules per unit time will reach the activation energy (2). Therefore the rate of reaction will increase. On the other hand if the temperature reaches a certain amount the enzyme might denature and therefore no longer able to carry out the reaction.
My hypothesis was that the enzyme with the temperature closest to the average body temperature will react fastest. I would have to reject this hypothesis because the test tube with temperature 12 degrees celcius time was 1:05 and the test tube closest to the average body temperature 23 degrees celsius was timed at 3:07. In the end, test tube with temperature 12 degrees celcius had the quickest time and proved my hypothesis wrong. In lab 2 we were testing the enzyme reaction rate with different pH levels and my hypothesis was that the test tube with the pH level closest to neutral would react the fastest. The data collected said that the test tube with pH level 3.5 timed 3:56, pH level 9 tested 4:17, and pH level 7, tested 3:40. The pH level 7 reacted the fastest and proves my hypothesis that enzymes with pH levels closest to neutral will react
Enzymes are biological catalysts, chemical reactions. Enzyme may act are called substrates and molecules called enzyme converts these into different products. Enzyme are used commercially, for example, synthesis of antibiotics. The study of enzyme is called enzymology.
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
...f denaturing the enzyme, thus making it unable to function because its active site had been reshaped into a shape that did not correspond with the substrate, to allow for them to interlock. The denaturing of the enzyme took place in Test tube B at 7 ½ minutes. The rest of the reactions in the other test tubes were continuing to react. All reactions maintained a very opaque colour and only when the hydrogen peroxide was added to the solution did the contents of the test tube clear up slightly and become more transparent in colour. The transparency of the solutions within the test tubes at the end of the experiment was because of the water that had been produced from the breaking down of the hydrogen peroxide which forms water (H2O) and oxygen (O2). The water diluted the solutions making them more transparent. These results are evidence in supporting my hypothesis.
Enzymes are proteins or RNA, ribonucleic acid. An enzyme speeds up a chemical reaction. Since the enzyme is not changed by speeding up a chemical reaction, the enzyme can speed up reactions again and again. In a process called catalysis, an enzyme takes what would have been a relatively slow reaction, and makes it faster than the reaction would have been without the enzyme. Enzymes also take the activation energy, which is the energy needed to start reactions, and shortens it. With the decrease in the amount of activation energy needed, reactions could occur more often, and less energy would be needed to begin each reaction. When an enzyme takes a substrate, which is a specific reactant, it changes the substrate in a specific way (Unity and Diversity 82). The active site on the enzyme is a specific shape, so the enzyme can only change certain substrates, the ones that fit into the enzyme’s activation site like a piece in a puzzle.
Enzymes work by lowering the activation energy required by molecules to start the reaction off. Enzymes also react (reversibly) with substrates (The molecule(s) that the enzyme is catalysing) this is done by forming Enzyme-substrate complex, which is then broken down into products. As well as being affected by temperature and pH enzymes optimum rate of reaction is also changed by competitive and non competitive inhibitors. Competitive inhibitors inhibit the enzyme so that enzyme-substrate complex’s cant form until it’s unblocked or there is a change in concentration in substrate, this means it takes longer to reach the optimum rate of reaction.
My prediction was very accurate as there were little products at room temperature, and according to my results the optimum temperature was only about 1ºC higher than my prediction. I also correctly predicted that the enzymes would denature after 40oC and that the graph would be exponential. Conclusion The graph starts with little carbon dioxide production at the low temperatures.
From looking at the results I can conclude that when the pH was 3 and
The aim of my investigation is to find out whether the increase of temperature increases the rate of reaction between the two reactants of Sodium Thiosulphate and Hydrochloric acid. I will then find out and evaluate on how temperature affects this particular reaction. Factors There are four main factors, which affect the rate of reaction that are considered as variables for the experiment I will be doing, they are the following: Molecules can only collide when two of them meet together.
to act on. The specific area where the enzyme binds with the substrate is called an activation
Feedback inhibition is when the product in the pathway stops the enzyme/the production of a substance. There are two main ways in which enzymes are inhibited. Either through