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…

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

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

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

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.45E

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help please answer in text form with proper workings and explanation for each and every part and steps with concept and introduction no AI no copy paste remember answer must be in proper format with all working
help please answer in text form with proper workings and explanation for each and every part and steps with concept and introduction no AI no copy paste remember answer must be in proper format with all working
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
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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).
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1. Reaction rate data of an enzyme, E, and a substrate, S, with increasing inhibitor concentrations are listed in the table below (Cs and C₁ represents the concentrations of the substrate and the inhibitor, respectively). Reaction Rates (μmol.Li¹.s¹) [CS] (mmol/L) [CI]=0 [CI]=0.25 [CI]=0.50 mmol/L mmol/L mmol/L 0.10 0.79 0.57 0.45 0.15 1.11 0.84 0.66 0.20 1.45 1.06 0.86 0.30 2.00 1.52 1.22 (a) Calculate Vmax (mmol.m³.s-¹). (b) Calculate Kм (g.mol.m³). (c) Describe the type of this inhibition.
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In general, reaction rates increase as the temperature increases. This is true for enzymatic reactions, up to a point. Describe the graph below and provide a reason for why the rate of enzymatic reactions stop increasing. Model 2: Effect of temperature on enzyme reaction rates Reaction Rate Stoob van WAH) 0 10 20 30 40 40 Temperature (°C) 50 50 60
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Which of the following is a general guiding principle behind modern biochemistry? Select one: O a. Monomers form dimers form polymers O b. Biological molecules only incorporate carbon, hydrogen and oxygen O c. Biological molecules always take straight-chain forms O d. Monosaccharides of all types move freely in and around all living cells e Carbon-based molecules are uniquely make-able by living things O e. Previous page Quiz navigation Time left 1:34:45 OL O O LO DELL

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