Yes, inhibitors can decrease enzyme activity by binding to the enzyme and preventing substrate binding. Activators can increase enzyme activity by binding to the enzyme and enhancing substrate binding or catalytic activity. Both inhibitors and activators can modulate enzyme activity by changing the enzyme's structure or function.
Yes, lowering the pH of the enzyme solution can affect the enzyme's activity. Enzymes have an optimal pH at which they function best, so altering the pH can disrupt the enzyme's structure and function, potentially leading to decreased activity or denaturation.
1. Temperature. 2. P.H level. 3. Enzyme concentration
Temperature, pH, salt concentration
It makes it grow very big
The enzymes become denatured
Yes, freezing an enzyme can affect its activity by denaturing it and changing its structure. Ice crystals can form and disrupt the enzyme's fragile structure, diminishing its function once thawed. It's best to store enzymes at their recommended temperature to maintain their stability and activity.
Ph level accelerates enzymes and temperature slows the process down
Factors such as temperature, pH levels, substrate concentration, and the presence of inhibitors or activators can affect the activity of an enzyme. Changes in these environmental conditions can alter the enzyme's structure, ultimately impacting its ability to catalyze reactions efficiently.
The pKA of enzyme affects its ionization which could alter enzyme activity. For pH < pKa, the value of vmax is constant and that for pH > pKa, vmax decreases; ie. enzyme activity starts to decline.
Temperature can affect enzyme activity by either increasing or decreasing the rate of the reaction. Low temperatures can slow down enzyme activity, while high temperatures can denature enzymes, leading to a loss of function. Each enzyme has an optimal temperature at which it functions most efficiently.
Temperatures affect speed of metabolism, enzyme activity, and the blood's ability to carry oxygen.