the reaction of glyceryl tristearate with water in the presence of of a lipase enzyme?
Practice-3 Write the equation for the reaction catalyzed by the enzyme lipase that hydrolyzes glyceryl trilaurate (trilaurin) during the digestion process. CH2-0-C-(CH2)10-CH3 CH2–0-C-(CH2)10-CH3 + 3H,0-ipase O CH2--0-C-(CH2)10 CH3 glyceryl trilaurate General Organic, and Biological Chemistry: Structures of Lile, 50 Karen C. Timberlake © 2016 Pearson Education, Inc.
7 What is the molarity of 24% NaOH in water? 8. What is the pH of 24% NaOH in water? 9 What is the molecular formula of glyceryl tristearate? 10 What is the molar mass of glyceryl tristearate? How many moles of glyceryl tristearate are present in 10.0 g of glyceryl tristearate? How many moles of NaOH are required to completely saponify 10.0 g of glyceryl tristearate? How many mL of 24% NaOH are required to completely saponify 10.0 g...
Draw the saponification process of glyceryl tristearate to give sodium stearate(soap) hint: stearin acid contains 18 carbons
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
Why is the V max of an enzyme-catalyzed reaction the same in the presence of a competitive inhibitor as it is in the absence of one?
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
Compared to the uncatalyzed reaction, which parameters change in the presence of an enzyme? All of the above change. O Keq
Part A The product of this reaction is CH2-0-C-(CH2)7-CH=CH-(CH2)2-CHz Ni, CH-0C-(CH3)3-CH=CH-(CHỊ)-CH, + 3H, 10 CH2-0-C-(CH2)-CH=CH-(CH2)-CH glyceryl trioleate. e glyceryl tristearate. glyceryl tripalmitate glyceryl tricaprate. Submit Request Answer Provide Feedback
Match each enzyme function with the corresponding pancreatic enzyme. Pancreatic amylase Pancreatic lipase Ribonuclease Answer Bank breaks down RNA into nucleotides breaks down starch into oligosaccharides and disaccharides breaks down triglycerides into fatty acids and monoglycerides
The enzyme carbonic anhydrase catalyzes the reaction CO2(g)+H2O(l)−→−HCO3−(aq)+H+(aq).CO2(g)+H2O(l)→ HCO3−(aq)+H+(aq). In water, without the enzyme, the reaction proceeds with a rate constant of 0.039s−10.039 s−1 at 25°C.25 °C. In the presence of the enzyme in water, the reaction proceeds with a rate constant of 1.0×106s−11.0×106 s−1 at 25°C.25 °C. Assuming the collision factor is the same for both situations, calculate the difference in activation energies for the uncatalyzed versus enzyme- catalyzed reaction.