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Ethyl Hexanoate Study

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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 …show more content…

The three-level-three-factor (Three levels as +1, 0, -1 and three factors as molar ratio, enzyme, temperature) CCD requiring 20 experiments were employed to optimize the significant parameters. The variables and their levels selected for the study of ethyl hexanoate synthesis were ethanol/hexanoic acid molar ratio (1:4 to 1:2), enzyme dosage (1 to 3 % w/w), reaction temperature (40 to 60°C). Table 1 shows the independent factors, levels and experimental design in terms of coded and uncoded …show more content…

It was well known that the collisions between enzyme and substrate molecules increased with an increase in temperature that result in an increase in reaction rate and thus the conversion. It was observed that with an increase in enzyme loading from 1-2% (w/w) increase in percentage conversion. Usually, an increase in enzyme loading increases the number of active sites and therefore more substrate molecules converted into products. The highest conversion could be attained when the enzyme loading was taken to be 2% in combination with the temperature 50 ˚C. 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

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Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be

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The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

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Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

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Dehydration of 2-Methylcyclohexanol Sura Abedali Wednesday 2:00 PM January 31, 2018 Introduction: Dehydration reactions are important processes to convert alcohols into alkenes. It is a type of elimination reaction that removes an “-OH” group from one carbon molecule and a hydrogen from a neighboring carbon, thus releasing them as a water molecule (H2O) and forming a pi bond between the two carbons1. In this experiment, 2-methylcyclohexanol undergoes dehydration to form three possible products: methylenecylcohexane, 1-methylcyclohexene, and 3-methylcyclohexene in a Hickman still apparatus. Adding 85% Phosphoric Acid to protonates the “-OH” group, turning it into a better leaving group and initiating the dehydration reaction.

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purpose the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster. Hypothesis I think that a warm environment would be best to make an enzyme’s reaction faster. because a protein can move faster in heat.

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By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.

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These enzymes have a secondary and tertiary structure and this could be affected by increases and decreases in temperature beyond the optimum temperature of the enzyme to work in. Mostly enzymes are highly affected any changes in temperature beyond the enzymes optimum. There are too

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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.

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INTRODUCTION: Lipase also called as triacylglycerol acylhydrolaseis an enzyme known for its enormous applications for industry and diagnostics. Their basic activity is to convert fats into fatty acids and glycerol. These enzymes are water soluble in nature. They also convert polar solvents into more lipolytic substances.

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