Catalytic Reaction Lab Report

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3.1 Preliminary optimization studies
3.1.1. Effect of reaction time:
Figure.3 represents the time progression for the enzymatic esterification of ethanol and hexanoic acid with 1:1 substrate ratio by Novozyme 435 (2 %) at 50 ˚C. It was observed that percentage conversion of ethyl hexanoate reached up to 73.6% in the initial 120 min. However, as the reaction proceeds further, a marginal change in conversion was observed after 120 min because of equilibrium of the reaction. This is attributed to the reversible nature of the esterification reaction. The slow rate of reaction after initial hours is due to collection over time of the reaction product on the enzyme this way reducing the surface area available for the reaction. Those moderate rate of reaction after introductory hours will be
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5) was made in the range of 313–333 K to find the activation energy as 25.76 kJ/mol (6.15 kcal/mol). The activation energy for enzyme catalysis (Ea) was in the range of 5–15 kcal/mol. This value lies within the typical value for enzyme catalytic reaction 27. Figure 6 showed acceptable linear fits and ΔH was appraised from the slope of the curves and ΔS was calculated from the intercepts. The values of ΔH, ΔS and ΔG obtained from the experimental data have been shown in Table 2. The negative value of ΔS indicates that the product is more ordered as compared to reaction. The positive value of ΔG indicates that the reaction was unspontaneous in nature. The positive value of ΔH shows that external heat requires to carry the reactants to the transition state so as to form the products. The positive value of ΔH for enzymatic reactions illustrate the endothermic nature of the reactions. The reaction temperature has a strong influence on the rate of the flavour production because the reaction was typical endothermic. Therefore, to initiate the reaction to reach the maximum conversion of ethyl ester, the reaction should be conducted at a suitable reaction

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