5- A(n) ________ is given of the glucose concentration in the sample.
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Environmental factors
________, such as temperature and pH, can denature and permanently alter the shape of enzymes.
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Non competitive inhibitors
________ can also bind irreversibly and reversibly, irreversibly deactivating the enzyme.
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substrate concentration
An increase in the ________ reduces the effect of these inhibitors, as more substrate increases their chances of successfully beating the inhibitor for the enzyme.
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excess OH
At a high pH, ________- ions neutralise positive charges.
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Percentage increase
________ in mass= (increase in mass (initial mass- final mass) ÷ initial mass) x 100.
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Enzymes
________ only catalyse energetically favourable reactions that would happen without their involvement.
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They are globular proteins
tertiary structure with hydrophilic R groups on the outside, making them soluble
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This is due to the differing behaviour of enzymes
they can fit either model more closely
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Activation energy is the minimum energy required for a reaction
to break the existing bonds and form new ones
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At this temperature, the increased kinetic energy causes vibration to increase to the point is breaks the hydrogen bonds, denaturing the enzyme
altering the active site so the substrate cannot fit
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At a high pH, excess OH
ions neutralise positive charges
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Percentage increase in mass = (increase in mass (initial mass
final mass) ÷ initial mass) x 100
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Rate of production (mg min-1) = increase in mass (initial mass
final mass) (mg) ÷ time (mins)
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The opposite is also true
an increase in inhibitors lowers the reaction rate
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These bind to the enzyme at an ‘allosteric site‘
a site other than the active site, therefore they do not compete with the substrate
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1
The reactants are allowed through the semipermeable membrane, in glucose detection this is glucose and oxygen
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2
Enzyme-substrate complexes are formed between glucose oxidise and glucose
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3
The product is made, gluconic acid and hydrogen peroxide
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4
This product is detected by the electrode, which converts the chemical energy to electrical
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5
A digital reading is given of the glucose concentration in the sample
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Inhibition
Decrease in the rate of an enzyme controlled reaction.
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Competitive
Inhibition that binds at the active site.
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Non-competitive
Inhibition that binds at the allosteric site.
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Feedback inhibition
Process where the final product of a metabolic pathways is a non-competitive inhibitor to the first enzyme in the process.
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Immobilised
Enzymes that are fixed in position.
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Alginate beads
Beads where enzymes can be held in place.
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Continuous flow
Technology where enzymes are held in place to constantly catalyse a product, such as lactase and lactose.
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Biosensor
When enzymes are used to calculate the concentration of molecules, such as in diabetes detection.
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Glucose oxidise
Enzyme used to detect glucose concentration.
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Gluconic acid
Product created and detected during glucose detection.
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Metabolic pathways
Enzyme controlled reaction sequences.
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Anabolic
Reactions that build up molecules.
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Catabolic
Reactions that break down molecules
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Basal
Metabolic rate when we are at rest.
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Enzymes
Biological catalysts that are tertiary proteins and are necessary for organisms to function.
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Extracellular
Enzymes secreted by exocytosis and used outside of cells, such as amylase in the mouth.
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Intracellular, in solution
Enzymes that act within a solution in a cell, such as glucose synthesis in the stroma.
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Intracellular, membrane-bound
Enzymes that act while attached to membranes, such as on the cristae where they transfer molecules necessary for ATP synthesis.
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Lock and key model
Enzymes specifically fit one particular substrate perfectly with no alteration needed.
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Induced fit
The enzyme is flexible, and changes shape so the substrate can fit and returns to its original shape afterwards.
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Activation energy
Minimum energy required for a reaction to occur, lowered by enzymes.
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Temperature coefficient
Measure of a reaction’s rate of change if the temperature is raised by ten.
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