The extent of reaction was found to decrease with an increase in temperature from 50 to 60ºC. Because at high temperature, the active site of the enzyme got denatured and no more accessible for distinguish substrate 25. However, with an increase in the enzyme amount above 2 %, decreases the percentage conversion. This can be attributed to disruption of enzyme tertiary structure and denaturation at high temperature
20 20 5 10 10 1.00 15.81 0.06 Graph Discussion: From the table and graph above it was observed that decrease in the concentration of hydrogen peroxide increased the time for the blue black colouration to appear, which gave rise to decrease in the rate of the reaction. The volume of distilled water added as shown in the table was to reduce the concentration of the hydrogen peroxide. The same trend was observed in the dilution of potassium Iodide. In the graph the volume of hydrogen peroxide was used as the concentration since concentration is proportional to volume. Conclusion It was clearly observed that the decrease in the concentration of hydrogen peroxide lead to increase in the reaction time and also decrease in the rate of the reaction.
Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable pH 3. Controlled Variables temperature, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable temperature 3.
The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds. It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.
We concluded that the rate of hydrolysis of (CH3)3CCl is directly proportional to water content in the solvent mixture. Aims of experiment • Determine the rate constants for hydrolysis of (CH3)3CCl in solvent mixtures of different composition (50/50 V/V isopropanol/water and 40/60 V/V isopropanol/water) • Examine the effect of solvent mixture composition on the rate of hydrolysis of (CH3)3CCl Introduction With t-butyl chloride, (CH3)3CCl, being a tertiary halogenoalkane, it is predicted that (CH3)3CCl reacts with water in a nucleophilic substitution reaction (SN1 mechanism), where Step 1 is the rate-determining step. The reaction proceeds in a manner as shown
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells. The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide.
Dev 2.11 R-Squared 0.9654 Mean 58.46 Adeq Precision 14.255 C.V. % 3.61 Co-efficient of determination (R2) for the model is 0.964, it indicates 96.54% of variability and the result of chance is 3.46%. Co-efficient of Variation (C.V) is found to be 3.61%, the reliability of the experiment is based on the lower value of C.V. An adequate precision value of 14.255 which was greater than 4, it indicates an adequate signal, and hence this model can be used to navigate the design space. Table 5 Data obtained from ANOVA ( Ethanol) Factor Coefficient Estimate df Standard Error 95% CI Low 95% CI High VIF Intercept 59.68 1 1.22 56.55 62.81 A-Temperature -6.84 1 0.75 -8.76 -4.92 1.00 B-pH 2.20 1 0.75 0.28 4.12 1.00 C-Stirrer Speed -0.39 1 0.75 -2.31 1.53 1.00 AB 3.77 1 1.05 1.06 6.48 1.00 AC 0.22 1 1.05 -2.49 2.93 1.00 BC 0.46 1 1.05 -3.18 2.25 1.00 A2 3.44 1 1.10 0.61 6.26 1.01 B2 -5.01 1 1.10 -7.84 -2.19 1.01 C2 -0.71 1 1.10 -3.53 2.12 1.01 Final equation in terms of actual
Effect of temperature on the reaction between the catalase and H2O2 Figure 1 shows that the optimum temperature for catalase to catalyze hydrogen peroxide is around room temperature (30℃) as it has a very fast reaction rate. The overall trend is that temperatures different from 30℃, will make the reaction rate decrease. Discussion This experiment supported the hypothesis, since catalase was the most effective with hydrogen peroxide when it was in an environment with a temperature of 30℃. It was expected that an extreme temperature would decrease the rate of reaction and results observed support that idea. With reference to figure 1, the peak performance of catalase was at 30℃, which was the closest to its usual environment of body temperature at 37℃ (Buddies, 2012).
The reaction mixture contained 100 µl of each of the extract solution in separate tubes (1 mg/ml) to which was added 0.5 ml of Folin-Ciocalteu phenol reagent, 1.5 ml of 20% (w/v) sodium carbonate and 10 ml of distilled water. After 2h of reaction at ambient temperature, the absorbance was measured at 765 nm and used to calculate the phenolic contents, using gallic acid as a standard. All experiments were performed thrice and the results were averaged and reported in the form of mean ± S.D.Then the total phenolic contents were expressed in term of gallic acid equivalents (mg GAE/g dry extract)
From the coefficient of friction, the relationship between the boundary coefficient of friction of solute and its solution concentration were acclimated to obtain the adsorption isotherms. The friction-derived adsorption results for each vegetable oils are shown in graph