The Environmental Factors That Effect Turnip Peroxidase

2009 words - 8 pages

Four environmental factors of enzymes were tested in lab. The changing of pH, substrate concentrations, temperature, and an inhibitor (NaCl) and the effects it hade on the enzyme turnip peroxidase. Enzymes are biological catalysts which increase reaction rates by lowering the activation energies of substrates. A substrate is a reactant that interacts with the enzyme. The enzyme and substrate can be viewed as the recently discovered "induced fit model", which suggests enzymes are flexible and dynamic things that change their shape so all these substrates (reactants) can become catalyzed when the activation energy is lowered and the reactions happen a lot faster. Sometimes in cells though it may not need a particular substrate (reactant) so an inhibitor comes into play. Inhibitors are basically regulators that inhibit (disallow) the process of catalysis to take place within a particular substrate. There are two types of inhibitors that occur in such reactions. Competitive inhibiters are remarkably similar to the substrate, so much that it can match interchangeably with the substrate, thus leading to a halt in the production of the intended product. Another variety of inhibitor is the allosteric inhibitors. Allosteric inhibitors change the shape of the enzyme by binding to a different site other the active site, which is the usual site for catalysis. Usually the allosteric inhibitors make contact with the side of the enzyme opposite the active site. In some occasions however an allosteric activator is introduced and functions by connecting to the enzyme in a way that it allows for easy access for a substrate to the active site. Allosteric activators are the opposite of allosteric inhibitors. These regulators (both inhibitive and active in function) help keep the cell in homeostasis by not allowing too much or too little of a needed or not needed product to be produced.. Enzyme activity is also regulated by cofactors which are either metal ions (e.g. Zn2+, Mg2+) or small organic molecules (e.g. coenzyme A, NAD, NADP, and many vitamins in our diet like iron). Cofactors main is to work together with enzymes to enhance the catalytic activity and by stabilizing the transition state. The transition state is the second of three steps of catylic action of an enzyme. The transition state and termination state are important in regards to cofactors because the cofactors allow interactions between the enzyme and substrate lowering the activation energy required.The goal of the following paper is to inform you the reader on how environmental conditions such as temperature, pH, salt (an electrolyte), and how substrate concentration itself effects the rate of reaction and properties of turnip peroxidase. If optimal rates of reaction can be determined for each parameter, perhaps a farmer can grow his turnips more effective and efficiently rather than if he didn't know that surrounding temperature, pH, cofactors, and inhibitors can effect the outcome of how much...

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