(Original post by coolguy)
does any1 know any detailed science why the rate of reaction of enzyme activity increases as concentration of hydrogen peroxide increases. please I need some very detailed scientific knowledge.
ok, a quick scan reveals that the people here suck at biology.
this is GCSE stuff!
The Hydrogen Peroxide is your substrate. That is to say it's the molecule that the enzyme is acting upon. The enzyme will break it down to water and oxygen. That's why you often meaure it by O2 collected, or number of bubbles per min etc
Think of it like this. The enzyme can do a maximum speed of breakdowns per minute. It's a maximum speed because that is the time it takes to
get the h202 into the enzyme, the reaction to take place, it to leave, and another to replace it.
Now look at that list again
1) H202 bind to active site of the enzyme
2) breakdown reaction to occur
3) breakdown products released (water and oxygen)
4) Another h202 binds to active site
If you keep temperature and ph constant (and dont do anything like add salts etc) then steps1,2 and 3 will be constant rate. They won't change.
Step 4 of course relies on how much h202 there is about in the solution.
Molecules don't line up ready to be broken down.
It's more like a school playground when you play 'kiss chase' everyone is running around randomly, and sometimes someone bumps into the kisser (the enzyme).
The more people there are, the more likely someone will be kissed (broken down)
The maximum reaction rate (at given temp and ph) is the point where the kisser is kissing as fast as he/she can. Having more people (substrates) won't mean a fast rate.
Hope that helps