Question 6Scenario:The 2nd year Food Science & Technology experienced EB during pressing of juice from Granny Smith. However, you advisedthem to pasteurise the second batch immediately after pressing. However, after cooling and filling in bottles, they noticed a bitof browning in the juice. They did a guaiacol test, but the it proved negative for any presence of enzymes.Students are now puzzled at how the juice is brown although enzymes were deactivated.Question:Which of the following browning reaction took place. Select the correct one from the list below?A Melanosis.B) Caramelisation.Maillard reaction.(D) Ascorbic acid degradation.

Answered: Question 6 Scenario: The 2nd year Food…

Introductory Chemistry: A Foundation

9th Edition

ISBN:9781337399425

Author:Steven S. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Donald J. DeCoste

Chapter21: Biochemistry

Section: Chapter Questions

Problem 28QAP: . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate...

See similar textbooks

Similar questions

Explain the Enzyme assays for soils?
A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2
1. Penicillin is hydrolyzed and thereby rendered inactive penicillinase, an enzyme present in some penicillin-resistant bacteria. The molecular weight of this enzyme in Staphylococcus aureus is 29.6 kilo Daltons (29.6 kg/mole or 29,600 g/mole or 29,600 ng/nmole) The amount of penicillin hydrolyzed in 2 minute in a 10-mL solution containing 109 g (1 ng) of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. [Hint: Convert everything to the same concentration terms] Show all calculations and include spreadsheets and graphs to determine Km, Vmax and kcat for this enzyme. Make sure your final answers have correct units. [Another hint: Note that [S] and amount hydrolyzed are already in concentration terms. So you don't need to worry about the volume for calculating [S] and V. ] Penicillin concentration (microM) Amount hydrolyzed (nanoM) 1 110 3 250 5 340 10 450 30 580…
Suppose that you have an enzyme concentration at the molarity calculated in question 2 and the product that you monitor has a value of x = 6200 M1 cm1. You ran eight reactions and found the following: Reaction # [substrate] (μM) Slope (Abs/min) 0 0.000 2345678 10 0.163 20 0.288 60 0.586 100 0.740 200 0.920 500 1.078 1000 1.143 M-4.45x10-M Calculate the values of Kcat and KM for the reaction (remember to include units). Show your plot and your calculations.
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
. Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?
The acid-catalyzed hydrolysis of sucrose, C12H22O11 + H₂O + H+ -> C6H12O6 + C6H12O6 + H+ is known as "inversion of sucrose" because the angle, a, by which the solution rotates polarized light changes from positive to negative as the reaction proceeds (data from 30 degree C): t/hr a 0 78 2 71 4 12 18 24 42 65.10 44.60 32.40 22.45 2.30 48 -1.96 61 -9 86 95 -15.80 -17.25 -21.15 ∞ Use this data to show that the reaction is first order and determine its rate coefficient (at 30 degree C).
7. A group of Colby students discovered a hydrolase that cleaves cellulose. After purifying the enzyme, an assay was performed by adding 0.1 μM of enzyme to the cellulose substrate concentrations shown below to characterize kinetic properties. [S] 2 x 10-6 M 4 x 10-6 1 x 10-5 2 x 10-5 4 x 10-5 1 x 10-4 2 x 10-3 1 x 10-² 4 x 10-² V (umol/min) 28 40 75 95 112 128 139 140 141 A. Use the data in the table above to estimate KM and Vmax for the enzyme. B. What is the keat of this enzyme? C. What is the catalytic efficiency of this enzyme?
A1L TPN order is written for 400 mL 10% Dextrose, 300 mL 4.25% amino acids, and a total of 37 mL of additives. How much sterile water for injection should be added? a. 55 mL b. 137 mL c. 163 mL d. 263 mL
(4) Write short notes on teeth decay with proper chemical equations.
AH = - 1.2 kcal/mol; Kp = 16 nM OH 1 HO AH = - 6.0 kcal/mol; N. Kp = = 76 nM OH 2 HOl. AH = - 5.5 kcal/mol; Kp = 0.5 nM OH (iii) By considering the enthalpies given, what do you think this suggests about the target (e.g. the binding pocket of an enzyme) that the molecule binds to?
If %T for sample A is 0.005%T and for sample B it is 25%T at 10 minutes after adding enzyme, which of the two tubes shows enzyme activity? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a Sample B Sample A Cannot determine without further information

SEE MORE QUESTIONS

Recommended textbooks for you

Introductory Chemistry: A Foundation

Chemistry

ISBN:

9781337399425

Author:

Steven S. Zumdahl, Donald J. DeCoste

Publisher:

Cengage Learning

Fundamentals Of Analytical Chemistry

Chemistry

ISBN:

9781285640686

Author:

Skoog

Publisher:

Cengage

Chemistry for Today: General, Organic, and Bioche…

Chemistry

ISBN:

9781305960060

Author:

Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:

Cengage Learning

Introductory Chemistry: A Foundation

Chemistry

ISBN:

9781337399425

Author:

Steven S. Zumdahl, Donald J. DeCoste

Publisher:

Cengage Learning

Fundamentals Of Analytical Chemistry

Chemistry

ISBN:

9781285640686

Author:

Skoog

Publisher:

Cengage

Chemistry for Today: General, Organic, and Bioche…

Chemistry

ISBN:

9781305960060

Author:

Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS