The Question is from neet-chemistry surface-chemistry , and it was created by the author P SRAVAN KUMAR

Question

Which of the following statements is TRUE regarding the effect of temperature on enzyme-catalyzed reactions?

P SRAVAN KUMAR · Accepted Answer

## CORE INFORMATION
✓ **Answer**: A
## CONCEPT FRAMEWORK
 **Primary Concept**: Enzyme kinetics and the effect of temperature on enzyme activity.
 **Related Topics**: Enzyme denaturation, activation energy, reaction rate.
 **Prerequisites**: Understanding of enzyme function, collision theory, and the concept of activation energy.
## SOLUTION PATHWAY
**Given Information**:
  The question asks about the effect of temperature on enzyme-catalyzed reactions.
  Four options describe different relationships between temperature and enzyme activity.
**Method & Steps**:
 1. Analyze each option to determine its validity based on the principles of enzyme kinetics.
  Reasoning: Enzyme activity is influenced by temperature.  Increasing temperature generally increases the kinetic energy of molecules, leading to more frequent collisions between enzymes and substrates, thus increasing the reaction rate. However, excessively high temperatures can cause enzyme denaturation, where the enzyme's three-dimensional structure is disrupted, leading to loss of function and a decrease in reaction rate.
  Formula/Rule:  No specific formula is directly applicable, but understanding the relationship between temperature, kinetic energy, and enzyme activity is crucial. 
 2. Evaluate Option A: Increasing temperature increases the rate until denaturation. This is true.  The rate increases with temperature up to an optimum point, beyond which denaturation occurs, reducing the rate.
  Working:  The increase in reaction rate is due to increased molecular motion and collisions.  The decrease after the optimum temperature is due to the unfolding and inactivation of the enzyme.
  Key Point: The optimum temperature is enzyme-specific and varies.
 3. Evaluate Options B, C, and D: These options are incorrect because they present oversimplified or false statements about the temperature-enzyme relationship.
  Result: Option A accurately describes the relationship between temperature and enzyme activity.
  Verification:  The statement aligns with the general principles of enzyme kinetics and the concept of denaturation.
 ## OPTION ANALYSIS
A ✓: Increasing temperature increases the rate until denaturation. This is consistent with the general behavior of enzymes.  The rate increases due to increased collisions between enzyme and substrate, but high temperatures cause denaturation which reduces activity.
B :x: The optimum temperature is not always 37°C.  This temperature is optimal for many human enzymes, but it varies greatly depending on the enzyme's origin and function.
C :x: Enzymes are significantly affected by temperature changes. Their activity is highly sensitive to temperature variations.
D :x: Decreasing temperature generally decreases the rate of reaction, but it does not always do so.  At very low temperatures, the reaction rate approaches zero, but the enzyme is not necessarily denatured; it is simply less active due to reduced molecular motion.
 ## LEARNING AIDS
 **Common Mistakes**:
  1.Assuming a constant optimum temperature for all enzymes:  Optimum temperatures are enzyme-specific.
  2.Ignoring the effect of denaturation at high temperatures:  High temperatures can irreversibly damage enzymes.
 **Quick Tips**:
  1.Remember the bell-shaped curve representing enzyme activity vs. temperature.
  2.Associate high temperatures with denaturation and low temperatures with decreased activity.

P SRAVAN KUMAR · Answer

The correct Option is "Increasing temperature always increases the rate of an enzyme-catalyzed reaction until the enzyme denatures."

P SRAVAN KUMAR · Answer

The optimum temperature for an enzyme is always 37°C.

P SRAVAN KUMAR · Answer

Enzymes are not affected by changes in temperature.

P SRAVAN KUMAR · Answer

Decreasing temperature always decreases the rate of an enzyme-catalyzed reaction.

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