Toothpicks Controlled Enzyme

Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be

Cofactor- Molecules that aren’t proteins nor organic, but help make the reaction go faster when they connect to the active site. 9. competitive inhibitor- prohibits the reaction from taking place by going into the enzyme’s active site so the substrate can’t. 10.

There was a trickle of blood from the coffee able to Anna and a pool of blood under her mouth. During this test, the team had to pay very close attention to the simulated blood. In small bottles there was blood from each suspect of the crime scene, along with Anti-A Serum and Anti-B Serum. Two drops of blood were placed in the “A” well and the “B” well. Once the blood was dropped, the Anti-A and Anti-B Serum was dropped in the correctly labeled wells.

Introduction: Enzymes are needed for survival in any living system and they control cellular reactions. Enzymes speed up chemical reactions by lowering the energy needed for molecules to begin reacting with each other. They do this by forming an enzyme-substrate complex that reduces energy that is required for a specific reaction to occur. Enzymes determine their functions by their shape and structure. Enzymes are made of amino acids, it 's made of anywhere from a hundred to a million amino acids, each they are bonded to other chemical bonds.

The products are released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique geometric shape that is complementary to the shape of a substrate molecule, similar to the fit of puzzle pieces.

The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably

The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

Rationale: Enzymes are used to make reactions faster. When there is more substrate the enzyme will be forced to work harder to get rid of it faster. The problem is that eventually the enzyme hits a threshold where it becomes so saturated with substrate that it can’t go any faster,

purpose the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster. Hypothesis I think that a warm environment would be best to make an enzyme’s reaction faster. because a protein can move faster in heat.

Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).

5 water bath were set up each to10 °C. (5 were used do the experiment faster) 5 cm3 of starch solution were added into the 5 test tubes that were labeled test tubes. Then 5 cm3 of amylase enzyme was added into the other 5 test tubes that were labeled. Put one of the starch solution test tube (preferably the one labeled 1) and one of the test tube containing amylase into the water bath (10 °C).

H20 + 2 O2 This experiment will use 1% catalase solution and 3% hydrogen peroxide solution, both diluted into water so the reaction slows down. Temperature will be controlled in this experiment to change the reaction speed of the enzyme and the substrate, this is what the experiment is looking at. The effect of the temperature will be determined by how much gas is released in two minutes, which will change the pressure inside the test tube and will be measured by a gas

By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.

ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.