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28 Cards in this Set

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How are monosaccharides joined together?

Condensation reaction

Removal of water - between 2 OH Groups

What is the bond in carbohydrates?

Glycosidic bond

How are polymers separated?

Hydrolysis reaction

Adding water

What is a polysaccharide?

Many monosaccharides, joined together by condensation reaction/glycosidic bonds

Test for starch?

Add iodine solution - Turns blue-black

Test for reducing sugar?

Benedict Solution - Turns brick red

Test for Non reducing sugar

Heat with Benedict solution, there should be NO change.


Then add dilute hydrochloric acid this breaks the glycosidic bonds.


After, add sodium carbonate, and this neutralises the solution.


Heat again with Benedict solution, this should turn brick red

How is starch digested?

Salivary amylase in the mouth and pancreatic amylase in the small intestine breaks starch into maltose


Maltase in the lining of small intestine breaks it down to glucose

What is lactose intolerance

Person does not have lactase enzyme

Two types of proteins

Globular and Fibrous

What are globular proteins?

Soluble proteins with a specific 3D shape



Examples - enzymes/antibodies/hormones

What are fibrous proteins?

Strong/Insoluble/Inflexible material



Examples - Keratin/Collagen

What are building blocks for proteins?

Amino acids

How are amino acids joined together?

By condensation reaction, between the carboxyl group of one and amine group of another, which leaves a bond between nitrogen and carbon called a peptide bond

What is the primary structure of proteins?

Sequence of AA, polypeptide chain - held together by peptide bonds

What is the secondary structure of proteins?

The polypeptide chain coils which forms a helix, held by hydrogen bonds

What is the tertiary structure of proteins?

Secondary structure folds again which forms a 3D shape. Held together by hydrogen, ionic and disulphides bonds

What is the quaternary structure of proteins?

Made of more than one polypeptide chain

What is the test for protein?

Biuret Test - Turns purple

What is an enzyme?

It is a biological catalyst. It speeds up the rate of reaction without being used up

What makes an enzyme specific?

Has a specific active site shape, only complementary substrates can bind to the active site to form enzyme substrate complexes

What is the Lock and Key Hypothesis?

The active site is rigid which means only exactly complementary substrates can bind to form enzyme substrate complexes

What is Induced Fit Hypothesis?

The active site changes shape, the substrate binds to the active site to form enzyme substrate complexes

How can substrate concentration affect enzyme activity?

An increase in substrate concentration, increases the chance of successful collisions and this increases the production of enzyme substrate complexes. This continues until all the enzymes active sites are full

How can temperature affect enzyme activity?

An increase in temperature, increases the kinetic energy making the molecules move at a faster rate, this increases the chance of successful collision which will increase the chance of enzyme substrate complexes being formed. This continues until it reaches an optimum. After the optimum the bonds in tertiary structure break which lose the active site shape this means that the substrate is no longer complementary so no enzyme substrate complexes can be made. The enzyme is denatured

How can pH affect enzyme action?

If the optimum pH is altered then the bonds in tertiary structure break, lose the active site shape so it can no longer form enzyme substrate complex. The enzyme is denatured

What are competitive inhibitors?

A substrate with a similar shape to the the substrate and a complementary shape to the enzyme's active site, it binds to the active site, blocking it, preventing ES complexes to be formed

What are non competitive inhibitors?

A substance that binds to another site of the enzyme other than the active site, causes enzyme to change shape, so less ES complexes can form