Unexpected Enviromental factors On Enzyme Activity?

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The discussion centers on an experiment measuring how temperature affects the activity of the enzyme B-galactosidase. The experiment involved adding a substrate to the enzyme and measuring the resulting absorbance at 420 nm to determine the reaction rate. The expected graph of enzyme activity versus temperature typically shows a "U" shape, indicating an optimal temperature for enzyme function. However, the observed graph displayed two peaks: one at 37 degrees Celsius and another at 60 degrees Celsius. This raises the question of whether an enzyme can exhibit two peak levels of efficiency. The initial assumption is that enzyme activity increases with temperature until denaturation occurs, which should render the enzyme inactive. The discussion seeks clarification on the possibility of the observed dual peaks and what factors might contribute to this unexpected result.
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Hi all,

I am currently a college frosh taking cellular biology lab. In lab we did an experminet to measure how tempature effects enzyme activity. We put 1 mL of B-galactosidase (when a certain substrate is added to this enzyme, a yellow liquid (product) is formed). Then we use a Spec-20 to measure the absorbance of light at 420 nm, thus we can measure the rate of the reaction).

I know that a graph of enzyme activity (rate) vs. temperature should produces an upside down possion distributin ( or a funky "U" shape) This beacasue enzymes have a peak tempature at which they work best at.


On my graph, the curve contains two peaks, one at 37 degree (body temp) and the other at 60 degrees.

Can an enzyme have two peak levels of effcintcy. It does make sense to me. I thought that the rate at which enzymes process substrate increase with temaperature until the tempature is high enough to denature the enzyme rendering it inactive.

Thank your the help, it is greatly apperated
 
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At that temp,the enzyme should be denatured and completely useless. Could something else have caused the peak?

Nautica
 
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