Optimum temp of amylase was identified by incubation of the amylase together with starch at various temps for 10 mins. and stopped with HCI. The volume of added DNS is negligle. Volume Volume Volume Concentration of Temperature (°C) of of stock of stock starch distilled Absorbance amylase starch (mg/mL) water (uL) (mL) (mL) 1 1 10 9 0.0053 10 1 1 10 9 0.1309 20 1 1 10 9 0.1185 30 1 1 10 9 0.0531 40 1 1 10 0.0206 Using this graphically determine the optimum temp of amylase?
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- In glucose estimation using Benedict's Reagent, what is/are the chemical reaction/s that resulted in the white precipitate observed.During enzyme analysis to determine glucose concentration (sample used is corn syrup stock sol. and enzymes are glucose oxidase and peroxidase), what conditions must be in place to ensure accurate results for such coupled reaction?From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
- Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graphCalculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.
- The glucose oxidase (GOD) method is commonly used to determine blood glucose level. Explain, the principle of GOD method by regarding reactions.After determining the optimum pH, you are now tasked to determine the inhibitory effects of acarbose, a known anti-diabetic drug which acts an inhibitor of alpha-glucosidase, an intestinal enzyme that hydrolyzes starch to release glucose for absorption and energy usage of the body. You studied the rates of the enzyme at different glycogen concentrations with and without the presence of 0.10 mM acarbose. Below is the summary for this procedure. a) What is the Vmax, in arbitrary units, of the uninhibited reaction (without acarbose)? b) What is the KM , in mM, of the uninhibited reaction (without acarbose)? c) What is the type of inhibition?Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
- Convert the experimental glucose concentration provided in below from mM (millimolar) to g/100 mL. Glucose Concentration is in mM 1.927 mM. ● Take the 1/100 dilution factor into consideration ● M will open the doors for you to get to g. ● Once at M assume 1L of solution. (Hint: this will help you when converting from M to moles) ● You will also need to calculate the molar mass of glucose which has the formula C6H12O6In Fehling’s test, aldose are oxidized to aldonic acid. Kindly give the reaction and mechanism of Fehling’s test from glucose to gluconic acid and then to the positive result. What would the reaction be if the sample is a non-reducing sugar?Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)