Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
b. running the reaction at 75 °C

Question

Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
b. running the reaction at 75 °C

b. running the reaction at 75 °C

Accepted Answer

Hi, everyone. Welcome back. Our next problem says Chymotrypsin an enzyme that facilitates peptide bond hydrolysis functions optimally in a small intestine at a ph of 7.5 to 8.5. How would the enzymes be a enzymes activity be impacted under the following condition? Select the best answer. The condition is conducting the reaction at 90 °C. So we have choice. A, the enzyme activity will increase significantly due to the higher temperature providing more kinetic energy for the reaction. B the enzyme activity will remain unchanged because Chymotrypsin is stable across a wide range of temperatures. C the enzyme activity will decrease because the high temperature will likely denature the enzyme disturbing its secondary and tertiary structures. Or d the enzyme will become inactive as the high temperature will completely break down its primary structure leading to irreversible loss of function. So let's think about the information we're provided and what would happen at this condition of 90 °C. Well, we have an enzyme and we know that it functions within the human body and it functions in this ph range that we're given from 7.5 very slightly basic to 8.5. How is the enzymes activity impacted at 90 °C? Well, 90 °C is extremely hot. Note that since this is an enzyme that operates within the human body, within a small intestines, its optimal temperature could be expected to be body temperature which is 37 °C. So we're talking way above its optimal operate operating temperature. Now know that this, you know, question is sort of red herring something to kind of fool us, which is that we're given a ph range. I'm gonna put a little X over that to say we kind of ignore that because we're not given a ph condition, we're given a temperature condition. So we kind of can ignore this ph condition and focus on temperatures, temperature at which it normally operates at 37 degrees and the condition we're given of 90 degrees. So let's think about these answer choices. Well, it is true that as temperature increases, a lot of enzymatic activity increases as you have more kinetic energy, the molecules are more likely to encounter each other. But this is only up to a certain point at somewhere around 50 degrees. Celsius. Most enzymes, the enzymes that act in the human body begin to denature or come apart, lose that secondary tertiary, that 3d structure. So choice A is not correct when applying to this condition where we've got such a high temperature way above the point at which most enzymes become denatured. Choice B the enzyme activity will remain unchanged because chymotrypsin is stable across a wide range of temperatures. We're not given that information. The only information we're given is about ph range. So that doesn't really tell us anything about its temperature range. We just need to assume because it's uh active within the human body that it's a range around that 37 degree mark. So I see the enzyme activity will decrease because high temperature will likely denature the enzyme disrupting its secondary and tertiary structures. Well, this is correct. We haven't got through all our answers. So I'm going to put a little dot here for now. Let's look at the fourth one just to make sure it's not a better answer. Since we have a select the best answer of our directions. Choice D says the enzyme will become inactive because the high temperature will completely break down its primary structure leading to irreversible loss of function. Well, this one's tempting because 90 degrees is so hot, it may well be virtually inactive. But the explanation goes on to say the enzyme or the high temperature will completely break down its primary structure. But you wouldn't really expect that to happen. You just would expect to break down that 3d, those secondary and tertiary linkages. It would take more energy to break the primary structure, those linkages between amino acids. That's why we have this enzyme in the first place to break those bonds. So choice D is the wrong explanation. So we're looking at choice C that this activity will decrease since the high temperature will denature our enzyme disrupting those 3d structures. So our answer is indeed to C here and we will see you in the next video.

Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
b. running the reaction at 75 °C

Verified video answer for a similar problem:

Key Concepts

Enzyme Activity

Temperature Effects on Enzymes

Denaturation

Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?b. running the reaction at 75 °C

Verified video answer for a similar problem:

Key Concepts

Enzyme Activity

Temperature Effects on Enzymes

Denaturation

Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
b. running the reaction at 75 °C