Table 3 - DeterminationTube#Potato Expt.Temp.2c3c4c5cextract(mL)2222roomtemp20 °℃40 °℃75 °℃Boiling100 °Cof the optimum temperature of catechol oxidase enzyme.1st Absorbance0 min. at Expt.Temp.dH₂O Catechol(mL) (mL)000013131313Start Time: 4:20Absorbance:0.072Start Time: 4:25Absorbance:0.114Start Time: 4:25Absorbance:2nd Absorbanceafter 10 min. in ExptTemp.Absorbance:0.097Time for reading: 4:30Absorbance:0.128Time for reading: 4:33Absorbance:Subtract 1stfrom 2ndabsorbance0.0560.137Time for reading: 4:35Absorbance:0.1320-193Start Time: 4:27 Time for reading: 437Absorbance:0-1260.0230.0610.0293rd Absorbanceafter 10 more min. atRoom Temp.Time for reading: 4:40Absorbance:Based on the data from Table 2 answer these questions:Q10) What is the enzyme's optimum temperature? Answer:Q11) Use the difference between 2nd and 1st absorbance to support your conclusion for the optimum temperature.0.159Time for reading: 4:43Absorbance:0.119Time for reading: 4:45Absorbance:Subtract2nd from 3rdabsorbance0-209Time for reading: 4:47Absorbance:0.1150.031-0.0180.016-0.011

Enzymes are protein in nature serve as biological catalysts in living things. By decreasing the…

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 22P: Based on your residing of this chapter, what would you expect to be the most immediate effect oil...

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Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
Based on your residing of this chapter, what would you expect to be the most immediate effect oil glycolysis, if the steady-state concentration of gJucose-6-P were 8.3 mM instead of 0.083 mM?
In an enzymatic reaction, the equations that correspond with and without inhibition according to linewear-burk are calculated, these are with inh: 3.5x + 6 = y without inh: 3.5 + 10 = y. calculate alpha factor
J. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves collected before dawn had a much lower specific activity than the enzyme collected at noon. This difference persisted despite extensive dialysis, gel filtration, or heat treatment. However, precipitation of the predawn enzyme by 50% (NH4)2SO4 restored the specific activity to the level of the noon-collected enzyme. Suggest an explanation.
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. A. 0.10 per minuteB. 0.25 per minuteC. 0.50 per minuteD. 1.0 per minuteE. 2.0 per minute
Describe the propagation stage of peroxidation reaction by showing peroxidation of oleic acid. Peroxidation of arachidonic acid is 200 times faster than oleic acid. Briefly explain that observation.
The Beutler test is used to diagnose GALT (UDP-glucose uridyltransferase) deficiency in infants. Blood from the heel is spotted onto filter paper and the spot is then subjected to an enzyme assay. Galactose 1-phosphate, NADP+ and UDP-glucose are added as substrates to the dried blood. The increase in absorbance at 340nm is measured over time which corresponds to reduction of NADP+ to NADPH . The amount of GALT activity in the blood of patients is therefore measured by stoichiometric relationship to the amount of NADPH produced from NADP+. However, GALT does not directly reduce NADP+ as you can see in the above diagram. Instead, the glucose 1-phosphate product from this reaction is shuttled into the oxidative phase of the pentose phosphate pathway by enzymes also present in RBCs. Which three (or possibly more if you must) enzymes downstream of GALT allow for quantitative correlation of a product of GALT with the appearance of NADPH? What is the stoichiometric relationship…
An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.
The molar absorption coefficient of cytochrome P450. an enzyme involved in the breakdown of harmful substances in the liver and small intestine. at 522 nm is 291 dm3 mol-1 cm-1. When light of that wavelength passes through a cell of length 6.5 mm containing a solution of the solute. 39.8 percent of the light was absorbed. What is the molar concentrat ion of the solute?
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
RESULTS Experiment 1: Starch Digestion by Amylase Tube number A1 A2 A3 A4 Contents amylase, water Lugol’s Solution test result (color) Positive (+) or Negative (-) for starch digestion N/A, control N/A, control N/A, control Benedict’s Reagent test result (color) Positive (+) or Negative (-) for starch digestion N/A, control N/A, control N/A, control Other comments or possible errors? Experiment 1: Starch Digestion by Amylase Note on safety: goggles should be worn during the entire set of 3 experiments until clean up is complete. Label 4 test tubes A1, A2, A3, and A4. (“A” stands for amylase). To each of the test tubes, add the following: (20 drops = 1 mL). Test tube A1: 1 mL (1000 ml) amylase, 1 mL (1000 ml) distilled water Test tube A2: 1 mL (1000 ml) starch solution (shake the starch bottle before adding any, as starch grains tend to…
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute

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