Living creatures produce thousands of enzymes, and the reason for this is because; ‘most enzymes only catalyze one biochemical reaction’ (1), and many different enzymes are need to do this. Enzyme-substrate specificity, this is when ‘a typical enzyme only works on the substrates used in one reaction’ (1). This involves the substrate(s) that bind to the active site. Both active site’s and the substrate’s shape are a match. The reason for this is because; this allows the substrate to bind to the active site, which is known as the ‘lock and key model’.
On the surface of the enzyme is an active site that temporarily binds the reactants or substrates forming an enzyme-substrate complex. The catalytic action of the enzyme then converts the substrate to a product or products. This conversion can take the form of a synthesis (building more complex molecules), a decomposition (splitting of the substrate), an oxidation/reduction (addition or removal of electrons), or an isomerization (rearrangement of atoms within a molecule). When the product or products are released, the enzyme emerges unchanged and available to convert more substrate into more products. Since enzymes can be used again and again, they are effective even at low concentrations.
Various enzymes have unique shape and chemical composition that creates a site, called and active site. This is to allow connection between the enzyme and other molecules called substrates. The shape and chemical makeup of the active site provides an area for part of the substrate to connect with the enzyme. (Farabee, 2010) Part of the active site holds the substrate and part catalyzes the reaction. Some enzymes act on one substrate only, while other enzymes act on a family of related molecules.
Enzymes act as biological catalysts; they make chemical reactions to work quicker and remains unchanged when the reaction finishes. Therefore enzymes are used to speed up biological reactions in body. They can be working within cells and outside cells catalyzing metabolic reactions in human bodies. Enzymes are globular proteins; therefore they are soluble and easily transported in blood. Enzyme has an active site in a specific shape because of its tertiary structure.
Enzymes are proteins that are used to speed up these reactions without being consumed by them. The activity of these enzymes can be altered by changing their environments, such as enzyme specificity (speed only a reaction that contains their substrate), increasing and decreasing temperature, concentration level, or adjusting the pH level. Catalase is a catalyst that digests potent hydrogen peroxide and converts it into H2O and O. It is due to this hydrogen peroxide digesting ability that we used catalase in this experiment. To record the role that environment plays in the reaction of an enzyme, we exposed the enzyme to various changes in temperature, concentration, and pH.
Enzymes and temperature As the temperature increases, so does the rate of reaction, but very high temperatures denature enzymes. This graph shows how the rate of reaction changes due to increasing levels of heat. As the graph shows: at roughly 37ºC (body temperature) the rate of reaction starts to fall, and the rate falls rapidly as the enzyme is denatured. Enzymes and pH Like with heat, changes in pH levels can denature an enzyme, different enzymes work best at different pH levels. The pH level where the enzyme works best depends on where it is in the body.
Enzymes, as a subclass of catalysts, are very specific in nature. Each enzyme can act to catalyze only very select chemical reactions and only with very select substances. An enzyme has been described as a "key" which can "unlock" complex compounds. An enzyme, as the key, must have a certain structure or multi-dimensional shape that matches a specific section of the "substrate" (a substrate is the compound or substance which undergoes the change). Once these two components come together, certain chemical bonds within the substrate molecule change much as a lock is released, and just like the key in this illustration, the enzyme is free to execute its duty once again.
Procedure is to be repeated using temperature of 0o, 60o, and 80o C. Introduction Enzymes are single-chain or multiple chain proteins that act as biological catalysts with the inherent ability to promote specific chemical reactions in vivo, as well as in vitro. Like all catalysts enzymes work by lowering the activation energy required for the reaction to occur, this is achieved because enzymes facilitate the formation of the transition state from substrate to product. Enzymes have three distinctive characteristics: 1. High specificity The ability to select and thus promote a particular chemical reaction on a single or small number of structurally related molecules is a key aspect of enzyme mechanics. Invertase is the enzyme which catalyses the hydrolysis of the disaccharide sucrose, into the monomers of glucose and fructose; due to the high specificity of enzymes one would not expect invertase to catalyze the
JUN 24 2011 Aim To find out at what temperature does catalyse enzyme work best in and in what optimum temperature the rate of reaction increases. Theory Enzyme is a substance of protein that helps digest food all around our body. Enzymes have the ability to catalyse reactions in living organisms. Catalyse enzymes are found all around our body especially in our liver. Catalyse enzyme creates hydrogen peroxide in to oxygen and water.
Aasir Osman Enzyme Investigation - Effects of pH on the Activity of Catalase Aim: The aim of this investigation is to determine the effect of the inhibitor which is pH, on the enzyme catalase, which can be obtained from potatoes. *************8 Introduction: Enzymes are proteins that catalyse the speed of biochemical reactions in the body. They are responsible for all metabolic functions and are absolutely vital for life itself. Without enzymes, reactions would take place too slowly to keep you alive. These proteins are highly specific regarding what they do and under what conditions they do it in.