Lab Report
Results
Discussion
The type of enzyme protease is serine protease as the enzyme shows maximum activity at neutral pH (7.5). The activity of the enzyme showed maximum fluroscence at pH of 7 and the temperature of 25 degrees Celsius. Serine protease enzymes are active at neutral pH. Also, the activity of the enzyme was reduced at alkaline pH of 8.5 and also at higher temperatures of 42 degrees Celsius.
Yes, enzyme protease exhibits Michaelis-Menten kinetics. The graph represents rectangular hyperbola closely and therefore exhibits Michaelis-Menten kinetics.
With Inhibitor
y = 25.492x + 0.472R² = 0.9025
Vmax= 1/0.472= 2.12 micromole/minute
Km=25.492/2.12 =12.02 micromole
Without Inhibitor
y = 11.999x + 0.3637R² = 0.9059
Vmax= 1/0.3637 =2.75 micromole/minute
Km = 11.999/2.75 = 4.36 micromole
The type of enzyme inhibitor used in this experiment is a mixed inhibitor that binds to both free and substrated bound enzyme and may also interfere with both substrate binding and catalysis. As a result, with the inhibitor the Vmax decreases and Km increases.
The activity of the enzyme protease was adversely affected at very high temperatures of 42 degrees Celsius and higher pH of 8.5. The enzyme activity was highest at pH of 7.5 and temperature of 25 degrees Celsius (room temperature). The fluorescene was seen at the highest for test tube number 2 that was exposed to pH of 7.5 and temperature of 25 degrees Celsius.
The activity of serine proteases are maximum at neutral pH (around 7) and at room temperature. The activity of the enzyme is reduced at higher pH or lower pH and lower and higher temperatures. The results of the experiment are consistent with the protease data as maximum flurescence was seen in test tube 2 that had pH of 7.5 and temperature of 25 degrees Celsius.
