Add equal amount of benedict's reagent. Heat gently. Red/orange colour indicates presence of reducing sugars.
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What monosaccharides make up maltose?
Glucose and glucose.
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What monosaccharides make up sucrose?
Glucose and fructose.
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What monosaccharides make up lactose?
Glucose and galactose.
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What reactions join monosaccharides?
Condensation.
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What bond is formed when two monosaccharides join together?
Glycosidic.
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How do you test for non-reducing sugars?
Add benedict's reagant, heat gently, add dilute hydrochloric acid, add sodium hydrogencarbonate solution to neutralise acid, re-test using benedict's solution.
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What is the test for starch?
Add two drops of iodine solution. A blue-black colour indicates starch is present.
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Why do lactose-intolerant people experience cramping, diarrhoea and bloating when the consume milk?
Because the lactose can't be hydrolysed by enzymes so when it reaches the large intestine, microorganisms break it down, producing gas.
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How are peptide bonds formed in proteins?
A condensation reaction, combining an OH from carboxyl group of one amino acid with the H from the amino group of another. This makes water which is removed and a bond forms between a carbon atom and a nitrogen atom.
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What is the primary structure?
The sequence of amino acids.
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What happens if you changed the amino acid sequence?
Will not function.
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What is the secondary structure?
The shape which the polypeptide chain forms as a result of hydrogen bonds.
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What is the tertiary structure?
When the chains are twisted and folded even more to form a unique 3D structure held together by a number of different bonds. Allows it to be recognised by other molecules
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What is the quaternary structure?
Individual polypeptide chains linked in various ways and often associated with non-proteins.
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What is the test for proteins?
Add biruet reagent , mix, a purple colour shows protein is present, a blue colour indicates absence.
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What are enzymes?
catalysts lowering activation energy through the formation of enzyme-substrate complexes.
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What is the lock and key model?
A substrate will only fit the active site of one particular enzyme.
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What is meant by the induced fit model?
The enzyme is flexible.
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What effect does temperature have on enzyme activity?
Gives molecules more kinetic energy but too high can change the shape of the active site and stop the enzymes functioning altogether.
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What effect does changing the pH have on enzyme activity?
Alters the charges on the amino acids that make up the active site, the substrate cannot become attached. Change in pH can break bonds that maintain the tertiary structure- alters shape of active site.
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What happens as you increase the substrate?
Rate of reaction increases because more active sites are being filled but then it levels off because all the active sites become occupied at one time.
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What do competitive inhibitors do?
They have a shape similar to the substrate so can reversibly bind to the active site. Increasing concentration of the substrate, the effect of the inhibitor is reduced.
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What do non-competitive inhibitors do?
Attach to the enzyme but not the active site, altering the shape of the active site so it cant fuction.
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