T2.5 Enzymes Flashcards
Enzymes
- Globular proteins that work as catalyst
- Polypeptide that takes on a very specific 3D shape
Substrate
The thing getting broken down by the enzyme
Active site
Area that is designed to match the substrate
Enzyme-substrate specificity
Shape and chemical properties of active site/substrate match eachother
Interaction between charges on substrate and charges in active site
What does enzyme catalysis involve?
Molecular motion and the collision of substrates with the active site
Collisions (when dealing with enzymes)
The coming together of an enzyme and substrate
Why do collisions occur?
A result of random molecular movement (Brownian Motion)
Activation Energy
The amount of energy required to start a reaction
Denaturation
When enzymes lose their native structure
What conditions/factors can cause denaturation?
Temperature, pH, detergents, pressure, and salinity
How does temperature effect enzymes?
- Higher temperature -> more kinetic energy -> more molecular collisions -> faster reaction rate
- When enzymes denature:
- Really high temperatures -> intermolecular bonds vibrate and break -> proteins lose shape (denatures) and no longer function
Can you draw a graph of how temperature effects enzyme’s rate of reaction?
Link to graph
You better
How does the pH effect enzymes?
- If too acidic: Positive hydrogen ions will bond with the negative charges of the substrate or enzyme, thus changing shape and losing function
- If too basic: Negative hydroxide (OH) ions will bond with positive charges of substrate or enzyme, thus changing shape and losing function
How is enzyme rate affected by substrate concentration?
More substrate -> more collisions -> more reactions
What is the limitation of substrate concentration?
Enzymes have a max rate
(If theres 3 workers making sandwiches, they can only make 3 sandwiches at a time. If there are 50 people waiting for sandwiches, the max rate is still only 3)
Saturation point
The point where the enzymes are working as fast as it can. (Where the rate plateaus)
Can you draw a graph for increasing substrate concentration vs rate of reaction? Including saturation point??
Link to graph
You better
Immobilized enzymes
When the enzymes are kept from moving, making them very stable.
Advantages of immobilized enzymes
- Can easily be seperated from products of the reaction (stops reaction at ideal time)
- Can be recylced, saving costs
- Do not denature
- Increases stability to temperature and pH, reducing rate of denaturation and how ofter it needs to be replaced
- Substances can be exposed to higher enzyme concentrations, speeding up reactions
Explain the use of lactase in the production of lactose-free milk
Companies culture yeast to purify lactase
Milk products can be treated with lactase before consumption so lactose intolerant people can absorb milk sugars because it is already broken down while the rest of the nutrients are not effected
Kilactic yeast converts the lactose to lactic acid