substrate concentration‚ the enzyme is working at “maximum efficiency.” With a concentration at 40‚ it produced 2‚339 products. 2. The maximum velocity of a reaction is reached when the active sites are almost continuously filled. Increased substrate concentration after this point will not increase the rate. The reaction rate increases as substrate concentration is increased. It will soon level off though. 3. When the concentration is at low substrate‚ most of the enzyme molecules are not filled
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1. A) I would expect the active site of nylonase to consist mainly of polar amino acids with a few nonpolar amino acids as well because the substrate for nylonase is polar overall‚ but has many nonpolar bonds. What makes me think that the nylonase enzyme is polar is that the substrate that would bind to the active site of nylonase has extreme polarity between carbon and oxygen‚ and between hydrogen and nitrogen due to their differences in electronegativity’s‚ but it still has the nonpolar bonds between
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of an enzyme-controlled reaction. How do these factors affect the chemical structure and properties of the enzyme. Many things can affect the rate of enzyme activity. The temperature of the enzyme‚ the pH of the solution‚ the concentration of the enzyme‚ substrate and the product. Also‚ another affector is the number of competitive and non-competitive inhibitors. As I cannot explain them all‚ I have chosen to explain the effect of temperature and also the effect of inhibitors on enzyme activity
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to determine the optimum temperature range for the activity of the enzyme lactase. Extreme temperatures can have a detrimental effect on enzymes; very hot temperatures can cause the denaturation in the enzyme‚ which is the loss of protein structure. This causes a change in the shape of the enzyme leading to its inability to perform its function. As previously stated‚ the alternate hypothesis read: the optimal temperature range for lactase activity is between 23 to 25 ℃. The alternate hypothesis presented
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Research Question: How will an increase of FeSO4 concentration affect the activity of the enzyme catalase? Hypothesis: By increasing the concentration of FeSO4‚ there will be a decrease in the activity of the enzyme catalase because the Iron (ii) in the metallic ion will act as an inhibitor during the catalysis of the hydrogen peroxide into O2 and H2O. Introduction: We rely on oxygen to provide us with energy (ATP) and go through all the phases of aerobic respiration. However‚ oxygen can be
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Investigating the Effect of Concentration on the Rate of Enzyme Catalysed Reaction To investigate the effect of concentration on the rate of enzyme catalysed reaction I must know all the factors that affect it in order to investigate in this. Here are all the factors: Temperature- Enzyme like it warm but not too hot. Enzymes are biological catalysts‚ which speed up chemical reactions. They work most efficiently at the optimum point (37°C). If they are below 37°C they will work
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Is everything determined? Have I already been predetermined to write this two page response on a paper im hardly understanding but writing about anyway? Did God already know that on the twenty fourth day of January 24‚ 2013‚ nineteen years into my life know that I was going to be struggling on this assignment? I guess Mr. Hawking and I will never know. Lets take a moment to honestly think about it. Stephen Hawking wrote his book (in this case we are referring to his short excerpt in The Norton Reader)
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The Effect of pH on Enzyme Activity A piece of Solanum tuberosum (potato) was removed and mixed with distilled water in a blender. The resulting solution was filtered through multiple layers of cheese cloth to filter out the liquid by eliminating any 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
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measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm‚ a wavelength which is best for recording the absorbance values for the experiment. From the results‚ 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also‚ 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the ONPG
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