explain the results effect of temperature and pH on amylase activity Table 1 Effect of Temperature on the Hydrolysis of Starch Time (minutes) 15 °C 37 °C 65 °C 0 2 4 5 8 10 >3 >3 >3 >3 >3 >3 >3 >3 1.831 0.642 0.993 0.300 >3 >3 >3 >3 >3 >3 Table 2 Effect of Ph on the Hydrolysis of S trach Time (minutes) 3.0 7.0 11.0 0 2 4 5 8 10 >3 >3 >3 >3 >3 >3 >3 >3 >3 1.930 1.070 0.747 >3 >3 >3 >3 >3 >3

explain the results effect of temperature and pH on amylase activity Table 1 Effect of Temperature on the Hydrolysis of Starch Time (minutes) 15 °C 37 °C 65 °C 0 2 4 5 8 10 >3 >3 >3 >3 >3 >3 >3 >3 1.831 0.642 0.993 0.300 >3 >3 >3 >3 >3 >3 Table 2 Effect of Ph on the Hydrolysis of S trach Time (minutes) 3.0 7.0 11.0 0 2 4 5 8 10 >3 >3 >3 >3 >3 >3 >3 >3 >3 1.930 1.070 0.747 >3 >3 >3 >3 >3 >3

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter22: Gluconeogenesis, Glycogen Metabolism, And The Pentose Phosphate Pathway

Section: Chapter Questions

Problem 6P

See similar textbooks

Similar questions

Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.
Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
The maximum saturation, 28.3ug of enzyme in 25ml water catalyzes the oxidation of ethanol at a rate of 2.5mm/min. Calculate the kcat in units of seconds if the enzyme has a molar mass of 65kg/mol.
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…
Sodium fluoroacetate (FH2CCOO- Na+) is highly toxic. Patients with fluoroacetate poisoning accumulate citrate and fluorocitrate in their cells. Which enzyme is inhibited by fluoroacetate for this to occur? Explain.
A new drug, Proinebrium, that reduces Kcat (Ki = 2.0 uM) has been developed to treat ethylene glycol poisoning. (1) What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?
Malonate (p. 227) poisons the citric acid cycle because it inhibits succinate dehydrogenase. After reviewing its structure, describe how the inhibitory effect of malonate can be overcome.
Factors Affecting Enzyme Activity: Catalase 3. What is the marker for the enzyme’s optimum condition?
The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500 min^-1. From the results shown in the table, enumerate Km and total amount of enzyme present. What is the Km for this enzyme? What is the Vmax for this enzyme? And what is the [E]T for this enzyme?
Equation for the esterification of glycerol and three ethanoic acids
Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·mol