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Investigation into the extent to which heating the enzyme urease causes changes to its rate of reaction and inactivation of it. Introduction. Enzymes are biological catalysts. They speed up chemical reactions and catalyse metabolic reaction in the bodies of living organisms. Background Knowledge. Urease is found throughout the animal and plant kingdoms. Urease is an enzyme which increases the rate at which urea is hydrolysed to form ammonium carbonate. It’s richest natural source is in the Jack bean plant ( a legume). Urease Reaction = H 0 + urea 2NH + CO Enzymes are globular proteins and they only work with specific substrates. This is because the substrate has to actually fit into the active site of the enzyme. If it doesn’t fit, then there will not be a reaction or, if there is, it would be slower without the enzyme. This is often called the ‘lock and key’ theory. Another theory into how an enzyme works is the “induced fit” theory.This is probably more accurate, it says that the enzyme and substrate do have to fit together to start off with, but then the enzyme substrate complex changes shape to create a tighter fit. This is more accurate because it gives an explanation into why some enzymes are so specific: Not only does the substrate have to fit into the active site, but cause it to change shape and “lock it in” also. There are four main factors that affect the rate at which an enzyme catalyses a reaction.( Apart from inhibitors) pH, Enzyme concentration, Substrate concentration and temperature. Temperature shall be experimented on in this practical. Prediction I predict that as the temperature is increased, the rate of reaction will increase too. This is because the more heat added to the reaction, the more kinetic energy is gained by the molecules.
Approximate Word count = 1193
Approximate Pages = 4.8
(250 words per page double spaced)
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