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- 1. If you are a medical technologist, which of the four methods of glucose determination would you employ? why? 2. Do you think PFF should be part of enzymatic method of glucose determination? Explain your answer. 3.Describe the accuracy and specificity of Nelson-Somogyi method.1. Describe the role of sodium and phosphomolybdate reagent in Folin Wu method. 2. Describe the accuracy and specificity of Nelson-Somogyi method 3. Do you think PFF should be part of enzymatic method of glucose determination? Explain your answer.A catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. Ea
- If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.Using the attachment, Answer the following questions: Prepare a double reciprocal plot with all three experiments (lines) on the same graph. Use your graph, and then answer items 2, 3, and 4 below. 1. Calculate the Vmax or apparent Vmax for all three sets of data. Likewise, calculate the Km or apparent Km for each set. 2. For Inhibitor X, what is the mode/type of inhibition? 3. For Inhibitor Z, what is the mode/type of inhibition? By comparison of the apparent Vmax to the control Vmax, what is the value of α’, as defined in class? If Ki’ = 10 mM for this inhibitor, then what must the inhibitor concentration [Z] be?The Km value of an enzyme-catalyzed reaction and its Vmax is 70 mmol/min. What is the rate of the reaction of the reaction when the substrate concentration is 7 × 10−2 mmol/min? a. 35 mmol/min b. 50 mmol/min c. 60 mmol/min d. 70 mmol/min
- Please ASAP. Thank you. Explain these results in short answer form. Why was the slope zero for blank solution? What was the optimal concentration for peroxidase activity? Do these values make sense?2. The enzymatic reaction rate r is given by equation 2 below as a function of substrate concentration Cs and kinetics parameters KM and rmax. Using linear and nonlinear regression in excel, evaluate the kinetic parameter constants of a biosystem given the gathered data from a series of batch runsCalculate KI' of the inhibitor from the information given. All information may not be needed to calculate. K'm = (29Ki+1.45x10^-10)/Ki Vmax = 11.7 µMs-1 Kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM Inhibitor Concentration = 5x10^-12
- Paste your Microsoft Excel Graph of the kinetic analysis. Compute for Vmax and Km values and identify the mode of enzyme inhibition involved.Please help me with finding the hypotheses that are being testing in each of the three enzyme experiments(the three tables below), and predicting the results of each of the three experiments based on the hypotheses (if/then). The laboratory experiment is enzyme activity.Activity 2 You are required to culture and identified yogurt starter cultures, Lactobacillus bulgaricus and Streptococcus thermophilus from a diluted yogurt sample (1ml of yogurt was dissolved in 9ml of peptone water) and observed the growth rates of Streptococcus thermophilus under varying conditions. The standard media accepted by the International Dairy Federation of the yogurt species, L. bulgaricus and S. thermophilus are MRS and M17 agar, respectively. You are also required to carry out different staining and biochemical techniques to identify different medically important bacterial species apart from yogurt cultures. Produce a report that includes; Description of how you have carried out aseptic techniques to cultivate these microorganisms to obtain pure cultures of bulgaricus and S. thermophilus from the mixed population (explain the principles behind each aseptic techniques used) and confirmation of these bacterial species by performing Gram’s staining. Description of…
