An enzyme is a macromolecule that acts as a catalyst in which it speeds up reactions by lowering activation energy (Campbell 151,152). Activation energy is the energy that is required for a reaction to take place (Campbell 152). In the reactions there are substrates which are reactants that enzymes act on (Campbell 153). Enzymes bind to the substrates then creating an enzyme-substrate complex, and while the two are joined together the catalytic action of the enzyme changes the substrate to the product of the reaction (Campbell 153). An Enzymes environment effects its behavior greatly, all enzymes have an optimal temperature were reaction is greatest which is approximately 35-40 ˚C (Campbell 155). When an enzyme reaches a temperature too high
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Enzymes have a pH at which it is most active, which falls in the range of pH from 6-8 with some exceptions like pepsin, a digestive enzyme in the stomach, that works best at a pH of 2 (Campbell 156). Most other enzymes would denature at a pH of 2 because they belong in an alkaline environment with a pH of 8 and not an acidic environment with pH of 2. Lactase is a great example of this. Lactase is the enzyme that catabolizes (breaks down) the sugar lactose (a disaccharide) into the two monosaccharides, galactose and glucose. Lactase is mostly found in the small intestine, where the pH is around 7. Therefore it is reasonable to hypothesize that human lactase is optimally active at 37 ˚C and at a pH of …show more content…
Descriptive Stats of Cofactor Control Vs EDTA In Figure D the control refers to the microfuge tube containing water milk and lactase and EDTA refers to the microfuge tube containing EDTA milk and lactase. The chart show the results of glucose produced from lactase activity in each tube. The control has the greatest average rate of glucose production with a mean of 117.3mg/dL and EDTA has the lowest amount of glucose production rate with a mean of 9.0mg/dL Discussion The specificity of enzymes experiment tested putting lactase into similar solutions of its substrate (lactose and maltose), to see if lactase would still bind to the similar substrates with the same amount of binding capacity that it would have when bonding to its substrate (specificity of lactase). The way we determined the results was by the measurement of glucose produced when lactase acted with each substrate. Figures A and B are the results of determining specificity and the results clearly show that lactase is specific to lactose. The average production of glucose when lactase acted with lactose was 429.8mg/dL , while the average production of glucose between lactase and maltose was 39.1mg/dL meaning that the reaction between lactase and lactose was happening much more quickly than the reaction between lactase and maltose because the more glucose produced the faster the reaction is
Enzymes have a pH at which it is most active, which falls in the range of pH from 6-8 with some exceptions like pepsin, a digestive enzyme in the stomach, that works best at a pH of 2 (Campbell 156). Most other enzymes would denature at a pH of 2 because they belong in an alkaline environment with a pH of 8 and not an acidic environment with pH of 2. Lactase is a great example of this. Lactase is the enzyme that catabolizes (breaks down) the sugar lactose (a disaccharide) into the two monosaccharides, galactose and glucose. Lactase is mostly found in the small intestine, where the pH is around 7. Therefore it is reasonable to hypothesize that human lactase is optimally active at 37 ˚C and at a pH of …show more content…
Descriptive Stats of Cofactor Control Vs EDTA In Figure D the control refers to the microfuge tube containing water milk and lactase and EDTA refers to the microfuge tube containing EDTA milk and lactase. The chart show the results of glucose produced from lactase activity in each tube. The control has the greatest average rate of glucose production with a mean of 117.3mg/dL and EDTA has the lowest amount of glucose production rate with a mean of 9.0mg/dL Discussion The specificity of enzymes experiment tested putting lactase into similar solutions of its substrate (lactose and maltose), to see if lactase would still bind to the similar substrates with the same amount of binding capacity that it would have when bonding to its substrate (specificity of lactase). The way we determined the results was by the measurement of glucose produced when lactase acted with each substrate. Figures A and B are the results of determining specificity and the results clearly show that lactase is specific to lactose. The average production of glucose when lactase acted with lactose was 429.8mg/dL , while the average production of glucose between lactase and maltose was 39.1mg/dL meaning that the reaction between lactase and lactose was happening much more quickly than the reaction between lactase and maltose because the more glucose produced the faster the reaction is