Salt Concentration Effect on Reaction Rates

Salt engrossment Effect on Reaction placeEnzymes are proteins that catalysis chemical reaction to its highest speed. They do so by lowering the activation energy. Enzymes check out an spry settle where a substratum, in this case, the hydrogen peroxide binds to it and watchs into water and oxygen. Salt minginess changes the structure of the protein, therefore, cause the rate of the reaction to decrease. The main purpose of this bring was to discover whether the salinity niggardliness affects the rate of reaction. Turnip Peroxidases were used, known as enzymes which are implant in plants and animals. The hypothesis was that as the salt compactness increases, the absorbance rate decreases. This study was completed by running test of four different share salt concentrations, 0%, 5%, 10%, and 15%. Using 0.5ml of peroxidase, .02 ml Guaiacol, 0.2 ml hydrogen peroxide, and a pH 7 buffer. Perform dickens tests per pipe for accuracy. Each tube was put in the spectrophotomet er at 500nm. tally to the data 15% salt concentration yield the highest absorbance.Introduction set ups and animals contain enzymes. Enzymes are proteins that are not consumed in the chemical reactions, but sort of it can speed up the reaction. Catalysis is an enzyme which is erect almost in all living jail cells especially in eukaryote cells (Cummings, 2005). It main act is to break down the hydrogen peroxide. enthalpy peroxide is just generate naturally in chemical reactions, but the cells have to get dislodge of it before it builds up in a large amount. A cell uses catalysis to break down the hydrogen peroxide into water and oxygen. Hydrogen peroxide forget going to feed into the catalysis and it is going to break that down into two products (Cummings, 2005). It does that at very incredible rate. Basically, an enzyme contains an mobile site. This active site is part of an enzyme where there has a hole in it. The substrate will than fit into it. The substrate is hydrogen peroxide. The enzyme basically tugs on substrate and breaks it down. Enzymes are very important in the chemical reactions, without them the reaction will occur at the lower rate. There are two types of inhibition. banning can either be competitive, that is where a chemical is blocking an active site or the allosteric, where the enzyme is actually changing the shape of its active site, ineffective the reaction to take place (Hosoya, 1960). An enzyme itself never changes its shape, unless the active site does. However, its unique structure of protein under specific circumstances can substantially be denatured. An enzyme needs to be in certain atmosphere to be more affective. One of the factors that can effect the enzyme reaction is salt concentration (Cummings, 2005). Salt concentration has to be in its intermediate state for an enzyme to construct properly. For instance, if the salt concentration is too high, consequently the enzyme site will be blocked by the salt ions (Huyste e, (1987). Therefore, it will lower the reaction military action rate. The main intention of this prove was to figure out the salt concentration and its effect on enzymes. To perform this experiment, use the turnip peroxidases. Peroxidases are an enzymes found in plant and animal cells (Gjesing, 1985). Because salt concentration denatures the enzyme we did an experiment to learn how the salt concentration would effect the reaction. It is believed that the increase in salt concentration will lower the absorbance rate of turnip peroxidases.MaterialsIn this experiment, the resolution materials that are needed to perform this lab are Enzyme Solution 5 g turnip blended into 500mL water (1% solution) and then filtered through a p2 filter, substratum Solution NaCl (0%, 5%, 10%, and 15%), Indicator Solution Guaiacol, caramel brown Solution pH 7 buffer (distilled water), and Hydrogen peroxides. The list of supplies that are need is follows a spectrophotometer, cuvette tubes, and micropi pette.MethodsPrepare a control test tube (called the blank), containing all of the ingredients 0.5 ml of turnip peroxidase, 0.5ml pH buffer, .02 Guaiacol, and put 0.2 hydrogen peroxide last, except the NaCl. Then, obtain the four additional cuvette tubes and start adding 0.5 ml (0 to 15%) of NaCl in each tube plus the same solution that control tube contains. Mix and put these tubes matchless by one in the spectrophotometer at 500 nm and record the absorbance every 15 seconds for 3 minutes. Repeat the trial for two times for each tube, then take the mean average.ResultsThe gush absorbance was at 15% concentrate (See routine 2). After the concentration passed 15% the reaction slowed gradually.DiscussionAs high percent of salt concentration was added the absorbance increased. This encountered because the salt concentration did not denature the enzyme (peroxidase), therefore, causing the enzyme to work its way out throughout until there was not enough enzymes to work with hydrogen peroxide. The data collected did not take for the hypothesis because the absorbance peak was at 15% salt concentration. As fictitious that the higher the salt concentration, the lower the absorbance would be. But that was not the case in this experiment. Salt concentration at 5 and 10% showed the lower peak, consequence that the presence of salt concentration actually lowered the reaction rate. It is the only 15% of salt concentration, where the peak was its highest. This could have happened because of the human error, miscalculation in finding the mean average, misreading the spectrophotometer or not having enough solution. If this experiment is to be repeated one of the question that should be addressed is what would happen if the higher than 15% of salt concentration was added, what would be the result? accede Legends and FiguresFigure 1. The Effects of Salt Concentration on Turnip Peroxidase Activity. Enzyme activity was measured using a spectrophotometer by recording the c hange in coloration of guaiacol to brown, indicating that hydrogen peroxide is complete.Figure 2. The Effects of Salt Concentration on Turnip Peroxidase Activity. Enzyme activity was measured at the high peak of 15% salt concentration.Literature CitedCampbell, Neil., Jane Reece (2005). Biology, 7th ed. Beth Wilbur. Benjamin Cummings,Publishing Menlo Park, California. pp. 150-157.Gjesing, K.W( 1987). Plant peroxidases. The Febs journal. 151 497-504.Hosoya, Toichiro (1960). Turnip peroxidase Purification and physicochemical properties ofmultiple components in turnip peroxidase. The daybook of Biochemistry. Vol. 47, No. 3.Huystee, R. B (1987). Some molecular aspects of plant peroxidase biosynthetic studies. TheJournal of Plant Physiology. 38 205-219.