What are two ways you can increase the rate of a chemical reaction?

Answer 1

The most effective way to increase the rate of reaction is to increase the temperature. This is effective up to a certain temperature (depending on the specific reaction and enzyme). Above that point the reaction may slow down (drastically) or stop entirely. Note that enzymes speed up a chemical reaction by physically binding with a substrate (or substrates) and causing the appropriate change (breaking apart a large molecule into two or more pieces, combining two substrates into one molecule, etc.) A substrate is a material (chemical, element, compound, whatever) that is undergoing a reaction. It is changed by the reaction. If the materials that are reacting are heated past an enzyme's tolerance, the enzyme undergoes what is known as "denaturation." This means that the molecule physically alters, losing the specific shape that allows it to function as an enzyme. As a reminder, heat is defined as random kinetic energy. That is, heat causes atoms, molecules, proteins, etc. to move around in a random fashion. Heat can speed up a reaction because it moves around the substrate and enzyme molecules faster, allowing them to "bump into" each other more often. By the same token, this random movement will, if great enough, shake up a molecule so much that molecule falls apart or alters in some way. High heat denatures the molecule. Another technique is to increase the amount of substrate and/or enzyme. Increasing the substrate or enzyme increases the rate of reaction because the two materials will bump into each other more quickly and frequently.

Answer 2

You can increase the rate of a chemical reaction by increasing the temperature, which provides more energy for reactions to occur, or by adding a catalyst that lowers the activation energy barrier for the reaction.

Answer 3

One way to increase the activity of an enzyme is to alter the temperature, to bring it nearer to the optimum for that enzyme.

Another is to adjust the pH, likewise to approach the optimum.

If there is very little of the enzyme present, increasing the enzyme concentration will also accelerate the overall process.

Answer 4

Take for instance you have added an irreversible inhibitor to a sample of enzyme and substrate, the reaction will stop completely. thus the enzyme is inactive at this point the way to regain the activity of this enzyme is to add new enzyme. Because they bind directly to the active site by covalent bonds, irreversibleinhibitors permanently render an enzyme inactive. Some drugs are irreversible inhibitors, including the antibiotic penicillin (which inhibits an enzyme involved in bacterial cell-wall synthesis) and aspirin (which inhibits cyclooxygenase-2, the enzyme involved in the inflammatory reaction).

Answer 5

Enzymes have temperature and pH range in which they function optimally.

If you change the temperature and pH so that they are at the optimal point - this will speed up the enzyme's activity.

Answer 6

First by latching onto the specific pair of substrate molecules that all, each, any and every enzyme is attuned to, it brings them into close proximity thereby lowering the Activation Energy of the chemical reaction involved below its 'usual' level.

In the Cell, enzymes provide 100% yield while reacting, this means that there are no useless by-products to clog 'things' up, and this alone speeds up all of the other cellular activities.

Answer 7

By altering the temperature to bring the enzyme closer to it's optimal temperature. Also, by altering the pH to bring the enzyme closer to it's optimal pH.

Answer 8

Heating increases the rate as does adding a catalyst.