The Digestive System

The digestive system is a tube through which food passes from the mouth where
food is ingested to the anus where it is egested. It consists of a series of organs,
each with a distinct structure and function. During the digestive transit food is
broken down into substances suitable for absorption into the bloodstream.
The gut wall has the same basic structure along its length. There are three main
layers:

An outer, muscular layer. Circular and longitudinal layers of smooth muscles

are present. Alternate contraction of these muscles moves food along the
digestive tract (peristalsis)

A middle layer of connective tissue - submucosa

An inner layer - mucosa

These three layers have different adaptations in different parts of the alimentary
canal. The adaptations are underlined below.

Oesophagus

Muscular tube carrying food from the mouth to the stomach

Stomach

Elastic and muscular organ which can expand

Highly folded mucosa

Gastric pits secreting gastric juices containing digestive enzymes (proteases)

Contraction and relaxation of the muscular wall mix the food thoroughly

Small Intestine

The site of chemical digestion and absoption of the products of lipids,

polysaccharides and proteins

Highly folded mucosa - arranged in villi (finger like projections to increase

surface area for absorption)

Epithelial cells lining the small intestine have a folded cell membrane microvilli to further increase the surface area for absorption

Large Intestine

The site of absorption of water

Undigested food matter forms faeces

Rectum
Faecal matter is stored here before egestion

Digestion

Large molecules (starch, proteins, TAG) are too big and insoluble to be
absorbed

Polymers have to be broken down into monomers

With help of hydrolytic enzymes - reaction requires H2O

Note: TAGs are not polymers but also need to be broken down

Different enzymes break down different food

o

Work best at body temperature (37)

Work in different conditions at different pH (stomach is acidic, intestine

is alkaline)

Hydrolysis
o

Proteins amino acids

Essential amino acids: cannot be synthesised and must be

present in diet

Non-essential amino acids: synthesised from essential amino

acids by transamination in the liver

TAG glycerol and fatty acids

Polysaccharides monosaccharides

Proteins

Proteins are made up by different combinations of 20 amino acids

o

Common structure

-COOH group

-NH2 group

Amino acids differ in their R-group

Tertiary structure
o

Complex globular 3D shape

Folding and twisting of polypeptides (H-bond, ionic bonds, disulphide

bridges)

Polypeptides contain many peptide bonds

Same amino acid sequence ALWAYS same shape

Bonds found in proteins

o

Hydrogen bonds

Between R-groups

Easily broken, but present in larger numbers

Ionic bonds

The more bonds, the stronger the structure

Between -COOH and -NH2 groups

Disulphide bridges

Between two sulphur-containing cysteine side chains

Strong bonds found in skin and hair

Denaturation
o

Destruction of tertiary structure, can be done by heat

Protein structure is lost and cannot reform dysfunctional

Background Reading: Structure of Proteins

http://www.chemguide.co.uk/organicprops/aminoacids/proteinstruct.html

What are enzymes?

All enzymes are globular proteins spherical in shape

Control biochemical reactions in cells

They have the suffix "-ase"

Intracellular enzymes are found inside the cell

Extracellular enzymes act outside the cell (e.g. digestive enzymes)

Enzymes are catalysts speed up chemical reactions

Reduce activation energy required to start a reaction between

molecules

Substrates (reactants) are converted into products

Reaction may not take place in absence of enzymes (each enzyme has
a specific catalytic action)

Enzymes catalyse a reaction at max. rate at an optimum state

Lock and key theory

o

Only one substrate (key) can fit into the enzyme's active site (lock)

Both structures have a unique shape

Induced fit theory

o

Substrate binds to the enzyme's active site

The shape of the active site changes and moves the substrate
closer to the enzyme

Amino acids are moulded into a precise form

Enzyme wraps around substrate to distort it

This lowers the activation energy

An enzyme-substrate complex forms fast reaction

E + S ES P + E

Enzyme is not used up in the reaction (unlike substrates)

Enzyme Activity
Changes in pH
o

Affect attraction between substrate and enzyme

Ionic bonds can break and change shape enzyme is denatured

Charges on amino acids can change ES complex cannot form

Optimum pH (enzymes work best)

pH 7 for intracellular enzymes

Acidic range (pH 1-6) in the stomach for digestive enzymes

(pepsin)

Alkaline range (pH 8-14) in oral cavities (amylase)

pH measures the conc. of hydrogen ions higher conc. will give a

lower pH

Enzyme conc
o

Proportional to rate of reaction, provided other conditions are constant

Straight line

Substrate conc.
o

Proportional to rate of reaction until there are more substrates than

enzymes present

Rate of reaction increases

Substrate binds to active site, but more enzymes are available

Rate increases if more substrate is added

Eventually, curve becomes constant (no increased rate)

Substrates occupy all active sites (all enzymes)

Adding more substrate won't yield more product, as no more

active sites are available

Increased Temperature
o

Increases speed of molecular movement chances of molecular

collisions more ES complexes

At 0-42C rate of reaction is proportional to temp

Enzymes have optimum temp. for their action (usually 37C in

humans)

Above 42C, enzyme is denatured due to heavy vibration that breaks

-H bonds

Shape is changed active site can't be used anymore

Decreased Temperature
o

Enzymes become less and less active, due to reductions in speed of

molecular movement

Below freezing point

Inactivated, not denatured

Regain their function when returning to normal temperature

Thermophilic: heat-loving

Hyperthermophilic: organisms are not able to grow below +70C

Psychrophiles: cold-loving

Monomer (-OH) + monomer (-H) polymer + H2O(l)

Condensation: monomers join to form polymers
o

Amino acids join to form a dipeptide (protein)

Two amino acids release -H and -OH groups (H2O)

Peptide bond forms between the alpha-carbon and nitrogen

Monosaccharides join to form disaccharides

Glycosidic bond forms between both monomers

Hydrolysis: break down of a polymer

o

Reverse of the condensation reaction

This is the process of digestion

Carbohydrates
Organic molecules which contain C, H and O
Bind together in the ratio Cx(H2O)y
Monosaccharides single sugar (monomer)
o

Ribose found in RNA and DNA

Deoxyribose part of nucleic acids

Glucose is the main energy source in brain

Fructose is found in sweet-tasting fruits

Disaccharides two sugar residues (2 monomers)

o

Sucrose (glucose + fructose) transport carbohydrates in plants

Maltose (glucose + glucose) formed from digestion of starch

Lactose (glucose + galactose) found in milk

Lactose intolerance

Polysaccharides many sugar residues (polymer)

o

Starch (alpha-glucose) main storage of carbohydrates in plants

Glycogen (alpha-glucose) main storage of carbohydrates in humans

Cellulose (beta-glucose) component of plant cell wall, important for

digestion

Starch
Consists of amylopectin and amylose (both are made of -glucose)
o

Amylopectin is branched via 1,6-glycosidic bonds

Amylose forms a stiff helical structure via 1,4-glycosidic bonds

Both are compact molecules starch can be stored in small space

The ends are easily broken down to glucose for respiration

Does not affect water potential as it is insoluble
Readily hydrolysed by the enzyme amylase produced by the pancreas and
present in saliva

Found in corn (maize), wheat, potato, rice

Biochemical Tests
Reducing sugars (all monosaccharides and some disaccharides) can be tested
for using Benedicts reagent. After placing the sample and the reagent in a
hot water bath a brick red precipitate will be produced if reducing sugars are
present.
Non reducing sugars require a negative result using Benedicts reagent. Add
hydrochloric acid to the sample and heat. Neutralize the solution using
sodium hydrogencarbonate and then test again with Benedicts solution. A
positive result will be found.
Starch can be tested for using iodine. In the presence of starch iodine will
turn blue - black.