As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.
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As the enzyme concentration increases the rate of enzyme activity increases up to a level where it becomes constant.
This is because the more the enzymes are available, the more substrates are broken in less time.
It then becomes constant as the substrate acts as a limiting factor, which means that there are not enough substrates to be broken down compared to the number of enzymes.
When you increase the enzyme concentration, the rate of enzyme reaction typically increases because there are more enzyme molecules available to catalyze the reaction. However, the rate increase may not be linear and can reach a point where all substrate molecules are already being acted upon, leading to enzyme saturation and no further increase in reaction rate.
So there are enzymes and there are substrates.
Enzymes dissolves substrates.
= So the more enzymes you have, the more substrates can be dissolved.
so theres more activity.
**but it doesn't work the other way--> more substrate does not increase enzyme activity.
Rebuttal - Substrates do not dissolve due to enzyme action eg glucose can be a substrate but clearly does not require an enzyme to facillitate it's diffusion! Answer Increasing the amount of substate means that it is more likely for the substrate to come into position on the active site of the enzyme. The substrate must locate the active site before the enzyme can work on it and turn it into a product. The more molecules of substate there are the more likely collisions with the active site are and so the greater the rate of enzyme activity up to a point. The point is where the enzyme is acting at it's full capacity, everytime the active site is empty another substrate molecule fills it right away. Increasing the substrate concentration after this point has no effect on the enzyme's rate of reaction.
Increasing enzyme concentration increases the number of collisions between the enzyme molecules and the substrate molecules. This increases the number of successful collisions and the number of enzyme-substrate complexes. Therefore the reaction rate is increased as well and enzyme activity is promoted.
because once lipase enzyme concentration is increased more substrates have a place where to bind, therefore the reaction rate increses. the more emzymes the better, until they actually have reached a maximum. Once there are no more free ubstrates to bind then the rate of reaction reaches a plateau
As the enzyme concentration increases the rate of enzyme activity increases up to a level where it becomes constant.
This is because the more the enzymes are available, the more substrates are broken in less time.
It then becomes constant as the substrate acts as a limiting factor, which means that there are not enough substrates to be broken down compared to the number of enzymes.
The easiest model to visualise this is the "lock and key model". Enzymes are the locks and substrates the keys. The keys are randomly bouncing around in space and by increasing their temperature you increase the speed and which they move. The faster the keys move the more chance they have of "hitting" a lock. This way enzyme activity increases with temperature as there is more liklyhood of the substrates finding the active site in a unit of time when the substrates are moving faster.
It can also be the case that the enzymes are free to move but in nature they can be bound to a fixed surface and so are unable to move.
Increasing temperature allows for more molecule movement, which in turn allows for great chance of a molecule to contact a enzyme. To much heat will denature the enzyme though.
An enzymatic reaction is an equilibrium reaction and the determiners of rate include enzyme and substrate concentration. An increase in either enzyme or substrate concentration will increase the rate of the reaction until one or the other component becomes saturated, beyond its ability to react or be reacted at a higher rate.
The higher the substrate concentration, the higher the rate of reaction, up till the point when the limiting factor is no longer the concentration of substrate but other factors like enzyme concentration of temperature.
Increasing the amount of enzyme used can increase the rate of the reaction, leading to a higher production of the product, up to a certain point. However, at a certain enzyme concentration, the reaction may reach saturation, and increasing the enzyme further may not significantly change the product yield.
Enzyme concentration has no effect on the rate of an enzyme-catalyzed reaction after reaching a saturation point where all enzyme active sites are occupied. At this point, adding more enzyme will not increase the reaction rate further.
If the substrate concentration is high, the rate of enzyme-substrate complex formation will increase until all enzyme active sites are saturated, which is known as enzyme saturation. This means that the rate of reaction will no longer increase with further increases in substrate concentration because all enzyme active sites are already in use.