Β Galactosidase Lab Report

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).

Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is

Since most of the known biological catalysts are proteins two criteria are generally used for establishing the existence of enzymes. The first is that the rate of a reaction in the presence of an enzyme is greater than the rate in its absence. Because the uncatalyzed rates of most biologically important reactions are effectively zero, the mere

Enzymes are biological catalysts that facilitate specific chemical reactions (Raven, et al., 2014). Enzymes do their job by

Organisms cannot rely entirely on spontaneous reactions to produce all the materials necessary for life. These reactions occur much too slowly. To produce these materials quicker, cells rely on enzymes, biological catalysts, to speed up these reactions without being consumed. (General Biology I, Martineau, Dean, Gilliland, & Soderstrom, Lab Manual, 2017, 43). To produce these materials quicker, the activation reaction much be lowered, a very important part of this lab. Each enzyme acts on a specific molecule, or set of molecules, called a substrate (43). The enzyme binds to this substrate, forming an enzyme-substrate complex. An enzyme is a protein whose structure is determined by the sequence of amino acids groups that

After reviewing the basics of enzymes and catalysis, we take a dive into the wonderful

Where kn represents the individual rate constants, E the enzyme, S the substrate, and P the product. When almost none of the product reverts to substrate the rate of the product formation i.e. the catalytic rate, V, is equal to k3 x [ES]. V is defined as the number of moles of product formed per second. Reaction rates are described by the Michaelis-Menton equation, shown in equation 4 (Boon, 2007).

Introduction Enzymes serve important roles in the biological processes that are undertaken in human bodies. Enzymes are most important as their role as proteins which speed up chemical reactions in the body, which make them catalytic proteins (Agarwal, 2006). The unique structure of enzymes allows them to fit into a specific type of chemical, called a substrate (Robinson, 2006). The functionality of an enzyme is determined by its active site. The active site of an enzyme is the location on the enzyme where the substrate binds to produce a substance (Robinson, 2006).

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).

B-galactosidase is a glycoside hydrolyse enzyme that initiates the hydrolysis of β-galactosidase into monosaccharaides through the breaking of the glyvosidic bond. B-galctosidase can also function to cleave fucosidases and arbinosidase but with lower efficiency. β-galactosidase was among the first hydrolyses to be discovered (Rouwenhorst et al. 1989). β-galactosidase is a very important enzyme in the human body, as it is an essential provider in the manufacturing of energy and a source of carbons through the breakdown of lactose to galactose and glucose. Lactase is the only enzyme that can break down lactose into components, glucose and galactose. However not all humans have the ability to break down lactose this is because not all humans can

Hence beta galactosidase is not produced. These results shows that IPTG acts as an inducer which allows the production of beta galactosidase by blocking the binding of the repressor protein to the operator site. Looking at Figure 2 which was the experiment data, the graph increased and then flattened out. This maybe due to the fact that the addition of Na2CO3 was done too quickly which killed the reaction prematurely. Also the time taken for induction to occur was significantly longer at 4 minutes which might point to an error when performing the experiment where ONPG was added at the wrong

The result is the high enzyme concentration had the fastest the catalytic

Enzymes are globular proteins that act as catalysts which affect the rate of chemical reaction without being destroyed or altered during the process. They are very effective in the body systems of organisms, an enzyme that catalyzes more than one thousand chemical reactions per second. But there are certain conditions that enzymes can work normally or efficiently, such as the temperature of the environment must be correct for each enzyme because different enzymes will have different optimum temperature ranges in which they can live; pH levels in the environment must also be correct because if the environment around the enzyme is too basic or acidic, the enzyme will quickly denature; substrate concentration also affects the rate of reaction

Enzymes are natural catalysts that work from the ability to increase the rate of reaction by decreasing the activation energy of a reaction. (Blanco, Blanco 2017) An enzyme can do this 10^8- to 10^10 fold, sometimes even 10^15 fold. (Malacinsk, Freifelder 1998) The substrate will momentarily bind with the enzyme making the enzyme-substrate complex, of which the shape of the substrate is complimentary to the shape of the active site on the enzyme it is binding with. There are two main theories as to how an enzymes and substrates interact, the lock-and-key model and induced fit theory. The lock-and-key model suggests that the enzyme has a specific shape that fits the substrate and only that substrate. The induced fit theory says the active site and substrate are able to change shape or distort for the reaction to take place with (Cooper,

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