The Effect Of Substrate Concentration On Enzyme Concentration

Because of the fact that reactions are catalyzed by enzymes when they randomly collide with substrate molecules, increasing the temperature would increase the reaction rate. Increasing the temperature further increases the vibrational energy of the enzyme molecules, straining the bonds that keep them together. Furthermore, when the temperature is higher, more bonds will break because of these strains, causing the active site of the enzymes to change too. Similar to pH, a change in the shape of the active site leads to the substrate not being able to fit perfectly, leading to the enzyme not being able to catalyze the reaction. Overall, an increase in temperature will cause the rate of reaction to increase initially due to the increased kinetic energy.

It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.

Enzymes are proteins that significantly speed up the rate of chemical reactions that take place within cells. Some enzymes help to break large molecules into smaller pieces that are more easily absorbed by the body. Other enzymes help bind two molecules together to produce a new molecule. Enzymes are selective catalysts, meaning that each enzyme only speeds up a specific reaction. The molecules that an enzyme works with are called substrates.

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.

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.

Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable pH 3. Controlled Variables temperature, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity 1.

40 celcius. At lower temperatures, sucrase activity begins to be inactive but quickly becomes active. At higher temperatures, sucrase activity Laboratory Report/ Natalie Banc/ Enzyme Activity/ Elizabeth Kraske/ 09.22.2016/ Page [2] of [4] starts to slowly become less active. 4. Was sucrase activity higher at 25 °C or 55 °C?

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.

These factors include the pH and the temperature of the solution (1). Most enzymes have a preferred temperature and pH range (2). The preferred temperature for catalase falls between the ranges of thirty five to fifty degrees Celsius (4). Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2).

These enzymes have a secondary and tertiary structure and this could be affected by increases and decreases in temperature beyond the optimum temperature of the enzyme to work in. Mostly enzymes are highly affected any changes in temperature beyond the enzymes optimum. There are too

Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration

Catalase and Temperature Introduction Background: Enzymes are catalysts which help reactions inside of organisms such as cells. Many different types of enzymes are used to catalyze different types of reactions. Enzymes are able to catalyze reactions that normally wouldn’t be possible under the specific circumstances in the cell such as the pressure or temperature of the cell. The way an enzyme works is it binds with the active site of a substrate and creates an enzyme substrate complex. The enzyme then breaks apart the bonds in a substrate and then leaves unchanged after the reaction.

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.

Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates. For the enzyme—factors affecting, the hypothesis concluded was if the temperature increases, than the enzyme activity will increase. This however was proven wrong, because enzymes become unstable at higher temperatures.

One reason for the efficiency and specificity of an enzyme is the way the enzyme interacts with reactant molecule also known as the substrate. The enzyme and substrate act together to form an enzyme-substrate complex. The interactions between the substrate and active site are frail, non covalent interactions (i.e. the substrate does not covalently bind to the active site but weakly interacts with it through interactions like hydrogen- bonding, van der Waals bonding. The orientation in which the two interact is highly constructive for helping in formation n of product after the formation of complex and going through different reaction steps ,it is actually the reason behind the specificity of the enzyme action as each enzyme has its own specific active site .which has a given and defined configuration with which no other enzyme can interact to form products due to that arrangement