unit 1 section 2 - Digestive system

?
What happens in digestion
we break down larger molecules into small molecules.
1 of 47
Give two examples of polymers in our food.
Proteins and carbohydrates.
2 of 47
What is hydrolysis?
Breaking down using water
3 of 47
Describe the oesophagus' role in digestion.
A muscular tube which takes the food from the mouth to the stomach by using waves of muscle contractions and mucus.
4 of 47
Describe the Stomach's role in digestion.
Walls produce gastric juice, walls churn the food mechanically, gastric juice contains HCL, pepsin and mucus.
5 of 47
What is the mixture that leaves the stomach called?
Chyme.
6 of 47
Describe the Small Intestine's role in digestion.
Chyme pushed along using muscular contractions, bile and pancreatic juices neutralise chyme, small molecules absorbed through villi.
7 of 47
Describe the Large intestine's role in digestion.
Absorb water and salt and minerals, bacteria here helps decompose undigested food, folded wall helps increase surface area.
8 of 47
Describe the rectums' roll in digestion.
To store faeces.
9 of 47
Describe the pancreas' roles in digestion.
To release pancreatic juices which contain a lot of enzymes and neutralise HCL
10 of 47
Two amino acids together are called what?
A dipeptide
11 of 47
More than two amino acids together are called what?
A polypeptide.
12 of 47
What are the 3 groups of an amino acid and what do they contain?
Amine group contains NH2, R group is the variable group, carboxy group contains COOH.
13 of 47
The bond between two amino acids is called what?
A peptide bond.
14 of 47
What type of reaction occurs when two amino acids bond?
A condensation reaction where h20 is removed.
15 of 47
Describe the Primary structure of a protein.
A sequence of amino acids in a polypeptide chain.
16 of 47
Describe the Secondary structure of a protein.
Hydrogen bonds start to form between the chain, making it coil into an alpha helix or beta pleeted sheet
17 of 47
Describe the tertiary structure of a protein.
Coiled up further with more hydrogen bonds forming at different points, for proteins made of single polypeptide chains, this is there final 3d form.
18 of 47
Describe the Quaternary structure of a protein.
The different polypeptide chains are all coiled up together very tight.
19 of 47
Describe the test for proteins.
Add sodium hydroxide, add copper sulfate solution, if there is a protein a purple layer will appear.
20 of 47
What are the monomers that make up carbohydrates?
monosaccharides
21 of 47
Give 3 examples of monosaccharides.
Glucose, fructose and Galactose.
22 of 47
On an alpha glucose is the hydrogen at the top of the bottom?
Top.
23 of 47
On a beta glucose is the hydrogen on the top or bottom?
Bottom.
24 of 47
What is bonded to the 6th carbon atom on glucose?
CH2OH
25 of 47
On carbon 3 is the hydrogen on the top or the bottom?
Top
26 of 47
On Carbon 4 is the hydrogen on the top or bottom?
Bottom.
27 of 47
What type of reaction occurs when two monosaccharides bond?
A condensation reaction.
28 of 47
What is the bond between two monosaccharides called?
A glycosidic bond.
29 of 47
On an alpha glucose, which carbons bond?
Carbon 1,4.
30 of 47
What is maltose hydrolysed into?
Glucose + glucose
31 of 47
What is Sucrose hydrolysed into?
Glucose + Fructose.
32 of 47
What is lactose hydrolysed into?
Glucose + Galactose.
33 of 47
Describe the test for reducing sugars.
Add Benedicts solution and then heat it up, if a reducing sugar is present then it will go from blue to brick red.
34 of 47
What is starch made from?
Long chains of glucose linked together by glycosidic bonds.
35 of 47
How is starch broken down?
Broken into maltose by amylase, then broken down into glucose by maltase.
36 of 47
What is the test for startch?
Add iodine dissolved in the potassium iodide solution, it will go from brown/orange to blue/black.
37 of 47
What do enzymes do to a reaction in terms of energy?
The lower the activation energy so less energy in needed to start the reaction.
38 of 47
How do enzymes lower the activation energy?
substrates bond to the enzymes active site, the enzyme applies pressure/strain which means the substrate is easier to break apart.
39 of 47
Describe the lock and key model.
The enzyme is a fixed/rigid structure that has an active site the exact shape of the substrate.
40 of 47
Give two limitations of the lock and key model.
Suggests the enzyme is rigid when its fluid, suggest enzyme has only one bonding site.
41 of 47
Give two strengths of the lock and key model.
Simple to understand, Gives basic understanding of how enzymes work.
42 of 47
Describe the induced fit model.
Enzyme active site will mould around the substrate as they go to bond because the enzyme is fluid.
43 of 47
Give a limitation of this model.
More complicated to understand,
44 of 47
Give two strengths of this model.
Gives more accurate picture, more detailed.
45 of 47
What is a competitive inhibitor?
same shape as the substarte so bonds with the active site stopping the substrate from bonding
46 of 47
what is a non competitive inhibitor?
Bonds to somewhere else on the enzyme, this changes the overall shape of the enzyme so the substrate cant bond to the active site still.
47 of 47

Other cards in this set

Card 2

Front

Give two examples of polymers in our food.

Back

Proteins and carbohydrates.

Card 3

Front

What is hydrolysis?

Back

Preview of the front of card 3

Card 4

Front

Describe the oesophagus' role in digestion.

Back

Preview of the front of card 4

Card 5

Front

Describe the Stomach's role in digestion.

Back

Preview of the front of card 5
View more cards

Comments

No comments have yet been made

Similar Biology resources:

See all Biology resources »See all Digestion and enzymes resources »