Free

Enzyme kinetics - Assignment Example

Comments (0) Cite this document
Summary
When the catalytic site becomes empty, more substrate is available to bore and undergo reaction. Vmax is the maximum rate of reaction and denotes the rate of reaction when the…
Download full paperFile format: .doc, available for editing
GRAB THE BEST PAPER93.8% of users find it useful
Enzyme kinetics
Read TextPreview

Extract of sample "Enzyme kinetics"

Enzyme Kinetics al Affiliation) Kinetic Properties of Enzymes a) i) The rate of the initial reaction The reaction rate of an enzyme-catalyzed reaction varies with substrate concentration. The common form of the equation is given by:
Vo = Vmax (S)
KM + (S)
Where: Vo = initial reaction velocity
Vmax = maximal reaction velocity when all enzyme active sites are filled with substrate molecules
(S) = Substrate concentration
KM = Michaels constant = K2+k3
K1
Rate = change in product
Change in time
Initial rate = 12-0 = 1.33 µmol min-1
9-0
ii) Effect of doubling the substrate
There is a hyperbolic relationship between the rate of reaction and the concentration of substrate.
The doubling of the concentration of substrate leads to the saturation of the enzyme by the substrate. When the catalytic site becomes empty, more substrate is available to bore and undergo reaction. Vmax is the maximum rate of reaction and denotes the rate of reaction when the enzyme is saturated. The relationship between concentration of a substrate and rate of reaction depends on the affinity of the enzyme for its substrate. This is expressed as the michaelis constant (Km) of the enzyme, which is an inverse measure of affinity.
iii) Time in minutes before 12 µmol of product forms in second reaction
Initially 1 = 1.33
2 = 3.99
Recall at the rate of 1.33, t=9
Therefore, t = (3.99/1.33) * 9mins = 27mins
Part C Enzyme Inhibitors
Enzyme inhibitors are molecules that interact with the enzyme preventing it from working in a typical way. A competitive inhibitor is a compound that resembles the molecular geometry and the chemical structure of the substance. Such inhibitors compete with the substrate molecule for the same site. We can measure the enzyme inhibitor ki through isothermal titration calorimeter. This involves titrating the inhibitor into a solution of enzyme and then measuring the heat released. Another way of measuring inhibitors is through Michaels Menten equation. Here, we need to observe an enzyme activity under a variety of substrates and concentrations. We can then plot the fitting data on graphs using Line weaver-Burk (Leskovac, 2003).
Part D (Short answer question)
100 mm = 1 L (def of molarity)
100mm in 1000 ml of the solution
Y = 10 ml
Y = (10*100)/1000 =1mol
75 g of glycerin =1 mol glycerin
Therefore, the solution contains 75 mg of glycerin.
References
Leskovac, V. (2003). Comprehensive enzyme kinetics. New York: Kluwer Academic/Plenum Pub. Read More
Cite this document
  • APA
  • MLA
  • CHICAGO
(“Enzyme kinetics Assignment Example | Topics and Well Written Essays - 250 words”, n.d.)
Enzyme kinetics Assignment Example | Topics and Well Written Essays - 250 words. Retrieved from https://studentshare.org/biology/1663184-enzyme-kinetics
(Enzyme Kinetics Assignment Example | Topics and Well Written Essays - 250 Words)
Enzyme Kinetics Assignment Example | Topics and Well Written Essays - 250 Words. https://studentshare.org/biology/1663184-enzyme-kinetics.
“Enzyme Kinetics Assignment Example | Topics and Well Written Essays - 250 Words”, n.d. https://studentshare.org/biology/1663184-enzyme-kinetics.
  • Cited: 0 times
Comments (0)
Click to create a comment or rate a document

CHECK THESE SAMPLES OF Enzyme kinetics

Enzyme Assays, Enzyme Kinetics

...?To Investigate and Measure Km and Vmax of ?-galactosidase Enzyme The main purpose of carrying out this experiment was to investigate and measure two parameters, Km and Vmax for ?-galactosidase enzyme. Furthermore the PH change effect on the enzyme activity was investigated as well. In general terms this was to introduce concepts related to enzyme kinetics. Introduction Enzymes are among several proteins generated in living cells to catalyze or accelerate the organism’s metabolic processes. Normally, enzymes are so selective and specific on the molecules they catalyze, referred to as substrate (Dixon, 1979).They normally...
6 Pages(1500 words)Lab Report

De-oxy-ribonuclease enzyme

...De-oxy-ribonuclease Enzyme Introduction Proteins are critical cellular components that play a diverse range of functions as many cell biologists have outlined. The complexity of the roles played by proteins and their interactions has remained intriguing. Moreover, the regulation of the production of such proteins as well as the processes involved in activation and deactivation of protein molecules have remained of great interests to cell biologists. The focus of this paper will be on de-oxy-ribonuclease, describing its function and structure. Proteins play critical roles in the cell, a factor that has helped scientists appreciate the salient significance of these molecules. Some cell proteins serve as...
3 Pages(750 words)Research Paper

Enzyme Kinetics

...ENZYME KINETICS To test how temperature, ph, substrate concentration, and enzyme concentration affect hydrolysis of lactose was theinterest of this research. This was done to learn the structure and function of an enzyme, to learn the relationship between substrates, enzymes, and products, to understand how different factors can affect the rate of an enzymatic reaction, to learn about lactose, lactase, and how to test for the presence of glucose with a Diastix, and to turn in a formal laboratory report. The researcher utilized Lactaid which is an over the counter tablet as a source of enzymes, known to particularly digest protein and...
14 Pages(3500 words)Lab Report

Kinetics Lab

...Kinetics Lab Procedure Preliminary Experiments Take a 50 mL beaker from the Glassware shelf and place it on the workbench. 2. Move it to the"top" of the workbench so the white wall is seen behind it which will make it easier to see the color change 3. Add 5.0 mL of 0.2 M KI solution from the Chemicals shelf to the beaker. 4. Dilute the 0.2M KI solution by adding 10.0 mL of water from the Chemicals shelf to the beaker. 5. Add 0.15 mL of the starch indicator from the Chemicals shelf to the beaker. When starch,(I), is present the starch indicator combines with it and makes the solution a blue-black color. 6. Add 5.0 mL of 0.2 M (NH4)2S2O solution from the Chemicals shelf to the beaker. The ammonium persulfate reacts...
5 Pages(1250 words)Lab Report

Enzyme Activity

...Investigation of Enzyme Activity Introduction In this paper the studies relating enzyme activity are considered. Different contexts regarding the activity of enzymes in pathogens, muscles and those affecting the critically ill patients are discussed from the findings of different studies. The enzyme activities that enhance muscle activities help in existence of pathogens and production and destruction of free radicals are discussed. The study of the activities of enzymes that help in existence of pathogens can help in developing the drugs, which decrease that activity and thus play an active role in preventing the pathogenical activities. The...
4 Pages(1000 words)Essay

Enzyme Linked Assays

...The enzymes are d according to the reaction they catalyze. For understanding the linked assay reactions, we can pick up one enzyme ly oxidoreductase. Oxidoreductases are enzymes that catalyze oxidation-reduction reaction. The substrate that is oxidized is regarded as a hydrogen donor. Enzyme-linked assays are immunoassays; specific antigen or antibody binding is used to identify and quantify substances. The antibody is linked to an enzyme that catalyzes a reaction. This is called enzyme linked immunosorbent assay. ELISA has many novel diagnostic uses, and in fact, an assay can be built up virtually to detect even a trace...
5 Pages(1250 words)Essay

Alkaline phosphatase enzyme

...ALKALINE PHOSPHATASE ENZYME Introduction Alkaline Phosphatase is a group of enzymes that is primarily found in the liver (isoenzyme ALP and bone (isoenzyme ALP-2). These enzymes are also produced by cells coating the intestines (isoenzyme ALP-3), the placenta, and also the kidney (in the proximal convoluted tubules). The test of Alkaline Phosphatase in the body measures the total amount of the enzymes that are released from the tissues of the above mentioned parts in to the blood. Due to this, the alkaline phosphatase enzyme works best at an alkaline pH of 10. As a result, the enzyme is inactive in the blood. The enzyme acts by splitting off phosphorous creating an alkaline pH. Function Alkaline phosphatase enzymes are phosphate... ...
5 Pages(1250 words)Essay

Chemical KInetics Chemistry

...of a reactant collide against each other, it is only a definite proportion of the collisions that result in a perceptible chemical change (Goldberger and Watson, 2004). These collisions are termed successful collisions, and possess activation energy. The idea of activation energy was introduced by Svante Arrhenius in 1889, and is the amount of energy needed to be gained by the reactant molecules to form the product. During the exact instant of collision, the pre-existing bonds are broken and new bonds formed. This results in the formation of the products of the reaction. The Maxwell-Boltzmann distribution law explains how the number of molecules that exist at a specific temperature is spread over a range of kinetic...
6 Pages(1500 words)Assignment

Enzyme Activity

...Enzyme Activity Introduction Enzymes are biological catalysts that are used in hastening biochemical reactions. Without the presence of enzymes, most chemical reactions in the body such as respiration would take a very long time to come to proceed. In addition, a lot of heat would be generated and lead to the destruction of living cells. Enzymes increase the rates of these reactions by lowering the activation energy of the reactions. Activation energy can be described as the least amount of energy that is needed for reacting substances to go through a reaction. An enzymatic reaction involves three main components namely the enzyme, the substrate (the...
8 Pages(2000 words)Lab Report

Enzyme lab

...on figure 1. The temperature effect is reversible in the case whereby the peroxidase is exposed to temperatures that negatively affect its function. This is through addition of many substrates to the active sites of the enzyme to enhance its activity. From the experiment, it is illustrated from graph in figure 2 with the constant slope from temperature of 40 C to320 C. further increase of temperature to 600C led to the reduction of the activity of the enzyme on the dye as a result of denaturing effect thus less color intensity. Conclusion Increase in temperature increases the rate of enzyme activity to a maximum level. This is because the kinetic energy is increased...
2 Pages(500 words)Lab Report
sponsored ads
We use cookies to create the best experience for you. Keep on browsing if you are OK with that, or find out how to manage cookies.

Let us find you another Assignment on topic Enzyme kinetics for FREE!

Contact Us