benzoquinone production when altering the pH and temperature of the reaction‚ as well as enzyme and substrate concentrations. We used a Spec 20 to evaluate absorbance at 540 nm. Absorbance represents rate of product formation. We tested the substrate catechol and the enzyme catacholase and recorded the product benzoquinone. The objective was to identify the optimal conditions for the enzyme catacholase. I predicted that the reaction rate will rise with increasing enzyme concentrations until an optimal
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Each tube had additional 47‚ 46‚ 44‚ 40‚ 32‚ 24‚ and 16 drops (one tube had no additional drops respectively. Each tube had drops of catechol added with respect to the numbered label (test tube 1 had 1 drop of catechol‚ test tube 16 had 16 drops‚ etc.). After these solutions were mixed‚ each tube was covered with Parafilm and inverted 3-4 times. The film was removed from the tubes and 30 drops of diluted potato juice was added
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Title: Preparation and Assay of Phenolase and Peroxidase from Sweet and Irish Potato Aim To design and conduct an experiment to demonstrate the presence of enzyme activity in the preparation provided. To examine the effect of the inhibitors provided. To test whether the other phenolic substrates provided can be oxidized by the enzyme preparation. To test for the presence of peroxidase activity in the enzyme preparation. To test the effect of the inhibitor provided on peroxidase activity
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Effect of Enzyme and Substrate Concentration on Reaction Rate by Zachary A. Poché Biology 155 Laboratory October 15‚ 2014 Lab Partners: Cade White‚ Hannah Ragas‚ Russheka Aremillion ABSTRACT In order to increase the reaction rate‚ substrates attach to the active site of enzymes which decrease the activation energy required to convert substrates to products. We examined the effect of enzyme concentration and substrate concentration on the overall rate of the reaction. To determine
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to find out how an increasing substrate concentration influences the rate of an enzyme activity; we obtained data from recording the absorbance of the samples which contain the same amount of potato juice (enzyme oxidase) and different amount of catechol (substrate) while holding pH and temperature constant. Our findings illustrate that the rate of enzyme activity is only influenced by substrate concentration at low level of substrate concentration‚ and as substrate concentration increases‚ the
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of the enzyme and the rate of the reaction. The browning of potatoes when they are peeled is caused by catecholase‚ an enzyme‚ as it facilitates a reaction between between catechol and oxygen. In this reaction‚ oxygen’s electronegativity separates 2 hydrogen atoms from catechol‚ oxidizing it and therefore converting catechol to benzoquinone molecules that forms long‚branched chains. The chains are the backbone of the red and brown pigments that cause darkening.
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The control group of this experiment was room temperature. The constant variables were‚ the amount of distalled water‚ catechol substrate‚ and potato extract in each tube was the same. (2ml) The size of the test tubes were the same also.
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large pieces in the solution. The solution created was catechol. Five different solutions were prepared as blanks with each test tube containing 6.0mL of a different pH (pH 4‚ pH6‚ pH7‚ pH8‚ pH10) of phosphate buffer‚ 1.0mL of the enzyme and 1.0mL of water. Five more solutions were prepared in the same fashion except without the 1.0mL of water. These five experimental solutions were capped and mixed by inversion. After mixing‚ 1.0mL of catechol was added to each of the five experimental solutions and
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The purpose of this experiment is to study how enzyme activity is affected by environmental conditions. Researchers tested the level of potato extract enzyme activity with 1-11 pH‚ varying temperature‚ catechol solution‚ hydroquinone solution‚ and different measurements of catechol. In Figure 1A and 1B‚ pH levels were tested with potato extract to see how pH would affect the amount of Benzoquinone is formed in the potato. Although it was hypothesized that enzymes would form Benzoquinone better in
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recalibrating it. The additional 4 experimental test tubes were composed of the same contents but 1 mL of the substrate catechol was added instead of the 1 mL of water (Table 2). These test tubes were labeled the same as the previous blanks. The spectrophotometer wavelength was set to 420 nm just like exercise A. After the spectrophotometer was adjusted using the blank A‚ the catechol was added to tube A. The tube was covered with paraffin and the absorption was measured within 5 seconds. The absorbance
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