Introduction: Within a cell, enzymes are used as a catalyst to increase the rate of chemical reaction. They do not consume themselves, rather they help in increasing the rate of reaction. Within the body, enzymes vary depending on their specific functions. For instance, hydrogen peroxide is a toxic chemical, but it
Student’s Name Instructor’s Name CHEM 202 Date of Submission Biochemistry Laboratory Experiment: Enzyme Kinetics Abstract The aim of the study is two-fold: to study the rate of absorbance with increasing concentration of glucose, and to measure the activity of enzyme yeast invertase on sucrose. In task 1, the product formation was measured using 3, 5-dinitrosalicyclic acid that reacts with glucose leading to a change in colour from yellow to reddish brown. In task 2, the enzyme kinetics of yeast invertase on sucrose was studied. The absorbance values of the corresponding volumes of the solutions were measured using a spectrophotometer. Michaelis-Menten curve and Lineweaver-Burk Plot were made in order to estimate the values of Vmax and Km
10 microliters of the sample is then added and the assay absorption is measured at 340nm. If absorbance was above 1.5, samples were diluted.
Introduction Enzymes are biological catalysts that facilitate specific chemical reactions (Raven, et al., 2014). Enzymes do their job by
Beta-Galactosidase and Western Blot 0 1. EMG 9 and EMG 26 contain strain _lac-_(I- Z+ Y+) and strain _lac -_ (I+ Z- Y-)respectively.Three genes huddled together on the chromosome are required for two strains of _E.coli_ to utilize lactose.Consisting of three genes, namely, _lacZ_, _lacY_ and _lacA_, the _lac_ operon orderly handles these genes to code specific enzymes necessary for the metabolism of lactose. The genes _lacZ_, _lacY_ and _lacI_ would code for beta-galactosidase, galactosidase permease and _lac_ repressor respectively. Regulation of _lac_ operon is also tight and the operon's negative control is made possible by _lac_ repressor (Hill, 1996). With the presence of _lac_ repressor, _lac_ operon will be deactivated and will
Enzyme Lab Using Jello INTRODUCTION: Enzymes are known as protein catalysts. The name protein catalyst suggests that most enzymes are made of proteins. A catalyst is a substance that speeds up chemical reactions without being consumed in the process. (Giuseppe, M 2002, p.69). After a reaction has been catalyzed, the catalyst can be used again to catalyze the same reaction. Enzymes reduce the activation energy (minimal energy) it takes for a reaction to take place. Enzymes can either catabolize (destroy), or anabolize (build up) a chemical system.
With both the stock substrate and varying enzyme solutions prepared, the Spec20 spectrophotometer was used to investigate the enzymatic activity of β-Galactosidase through an absorbance-based assay. Using LoggerPro software on the computer to analyze the absorption data, the Spec20 was calibrated before each run with 0.5 mL of the tested enzyme concentration at an absorbance of 420 nm. Data collection was then started, instantly followed by the addition of 0.5 mL of the stock 2.5 mM substrate solution, topping off the 1-mL cuvettes. Each of the nine varying enzyme concentrations were split between the team and run for a total of 10 minutes. Upon completion, data from each varying enzyme concentration was copied to a single Excel sheet and used
After the substrate solution was added, five drops of the enzyme were quickly placed in tubes 3, 4 and 5. There were no drops of enzyme added in tubes 1 and 2 and in tube 6 ten drops were added. Once the enzyme solution has been added the tubes were then left to incubate for ten minutes and after five drops of DNSA solution were added to tubes 1 to 6. The tubes were then placed in a hot block at 80-90oC for five minutes. They were then taken out after the five minute period and using a 5 ml pipette, 5 ml of distilled water were added to the 6 tubes and mixed by inversion. Once everything was complete the 6 tubes were then taken to the Milton Roy Company Spectronic 21 and the absorbance of each tube was tested.
Enzymes Lab Report Introduction Organisms cannot depend solely on spontaneous reactions for the production of materials because they occur slowly and are not responsive to the organism's needs (Martineau, Dean, et al, Laboratory Manual, 43). In order to speed up the reaction process, cells use enzymes as biological catalysts. Enzymes are able to speed up the reaction through lowering activation energy. Additionally, enzymes facilitate reactions without being consumed (manual,43). Each enzyme acts on a specific molecule or set of molecules referred to as the enzyme's substrate and the results of this reaction are called products (manual 43). As a result, enzymes promote a reaction so that substrates are converted into products on a faster pace (manual 43). Most enzymes are proteins whose structure is determined by its sequence of its amino acids. Enzymes are designed to function the best under physiological conditions of PH and temperature. Any change of these variables that change the conformation of the enzyme will destroy or enhance enzyme activity(manual, 43).
In order for maximal activity of E. coli β-galactosidase requires both Mg2+ and Na+ (Huber).
The main methods used were that of spectrophotometry, using light and standard curves. A urea enzyme assay was performed via separating the proteins so as to observe which of these proteins were specifically causing an effect on the absorbance and produce urea. Another technique used in the experiment was the generation of a protein standard so as to determine the concentration of protein in the liver extract mixture
INTRODUCTION Enzymes are biological catalysts that speed up chemical reactions, without being used up or changed. Catalase is a globular protein molecule that is found in all living cells. A globular protein is a protein with its molecules curled up into a 'ball' shape. All enzymes have an active site. This is where another molecule(s) can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, a product is produced. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate. It is said that the substrate is complimentary to their substrate.
Of the many functions of proteins, catalysis is by far the most vital. When catalysis is not present, most reactions in the biological systems take place very slowly to produce at an adequate pace for metabolising organism. The catalysts that take this role are called enzymes. Enzymes are the most efficient catalysts; they can enhance rate of reaction by up to 1020 over uncatalysed reactions. (Campbell et al, 2012).
Effects of Temperature, pH, Enzyme Concentration, and Substrate Concentration on Enzymatic Activity INTRODUCTION Enzymes, proteins that act as catalysts, are the most important type of protein[1]. Catalysts speed up chemical reactions and can go without being used up or changed [3] Without enzymes, the biochemical reactions that take place will react too slowly to keep up with the metabolic needs and the life functions of organisms. Catecholase is a reaction between oxygen and catechol [2]. In the presence of oxygen, the removal of two hydrogen atoms oxidizes the compound catechol, as a result of the formation of water [2]. Oxygen is reduced by the addition of two hydrogen atoms, which also forms water, after catechol is
Background Information Enzymes are biological catalysts naturally produced by living organisms which increase the rate of a specific biochemical reaction without being used up in the process. They are proteins of differing and complex three dimensional structures, constructed by sequenced amino acids which are pre-determined by the genes of their cells. As most enzymes are globular in nature, many are water-soluble with a spherical shape, unlike fibrous proteins which have different properties. All living organisms synthesise enzymes as they are an essential physiological component of life, responsible for a wide range of diverse functions; such as aiding in digestion, DNA replication, and glycolysis which leads to the formation of