Enzymes Flashcards
What are some the risk factors of heart disease?
high sugar diet lack of activity high cholesterol stress high blood pressure
What are some the risk factors of cancer?
Sunbathing Xray lack of fibre radiation infection reproduction
What are from the risk factors of both cancer and heart disease?
Smoking
alcohol
being overweight
genetics
How is food digested in the mouth?
Physical digestion by teeth
Amylase- starch -> maltose
What is the role of the stomach
Hydrochloric acid to denatured enzymes in pathogens
Protease- proteins -> amino acids
What is the role of the liver and bile duct?
Neutralises acid from the stomach
Emulsifies fat
What is the role of the pancreas?
Secretes pancreatic juices
Pancreatic amylase
What is the role of the small intestine?
Secretes enzymes from lining
Maltese
lactase
sucrase
(Hydrolyses enzymes)
What is the role of the large intestine?
Re-absorbs water
Absorbs nutrients
What monosaccharides make up maltase?
Glucose + glucose
What monosaccharide makes lactose?
Glucose + galactose
What monosaccharides make up sucrose?
Glucose + fructose
What is the Benedict’s test?
Used for testing reducing sugars
- Food sample dissolved in water
- And equal volume of Benedict’s reagent is added (copper sulphate)
- heat in a water bath
Blue = none Red = high
What is the test for a none reducing sugar?
- Carry out the Benedict’s test
- Add the same amount of the food sample and hydrochloric acid (hydrolyses disaccharide -> mono)
- Reheat the sample
- Add sodium hydrocarbonate
(Neutralises acid) - Retest with Benedict’s reagent
What’s the test for starch?
- Add sample into a test tube
- Add a couple of drops of iodine solution
Starch present= blue/black colour
What do all proteins contain?
Nitrogen or sulphur
Peptide bonds
What is the primary structure?
A sequence of amino acids
What is the secondary structure?
Chain of amino acid is an alpha helix are a beta pleat
Held together by hydrogen bonds
What is the tertiary structure?
Folds into 3-D structures hydrogen bonds ionic bonds disulphide bridges hydrophobic interactions
What is the quarternary structure?
Proteins greater than one polypeptide Either globular of fibrous Hydrogen bonds ionic bonds Disulphide bridges Hydrophobic interactions
Why is the order of amino acids important?
So the bond such as disulphide bridges can be made
Amino acids need to be in the right place
If the primary structure is incorrect so the tertiary structure and therefore the preteen will not function
What is the biuret test?
Add an alkali (KOH or NaOH)
Add copper sulphate
^ionisers peptide bonds
Proteins form a violet/purple colour
What are the properties of a globular protein?
Small molecule easily transported disulphide bonds hormones or enzymes Hydrophobic which makes it soluble
What are the properties of a fibrous protein?
Long strands secondary structure insoluble strong covalent bonds collagen (skin) keratin (hair)
What is the effect of pH on enzyme reaction?
The rate of reaction decreases rapidly due to less enzymes substrate complexes forming as the active site changes as the pH affects the ionic and hydrogen bonds in the tertiary structure
What is a competitive inhibitor
The inhibitor takes the place of the substrate and forms temporary bonds
What is a non-competitive inhibitor
The inhibitor binds to the site other than The active site and forms permanent bonds. This changes the shape of the active site
What is the lock and key theory
The substrate will only fit the specific Active site
complementary
The active site does not change shape
what is the induced fit theory
The enzyme active site is flexible and changes slightly to fit the substrate
Not quite complementary
Mould around substrate causing strain on bonds
How to increase the rate of enzyme reaction
More active sites( rate of reaction stops when all active sites are filled)
Increase concentration of substrate
