Biology 20 - Unit D8.1 Nutrients V2

Essential Nutrients
Chapter 8 - Digestive System

Unit D - 8.1
Goal
D1.2 : Students will describe the chemical nature of
carbohydrates, lipids and proteins and their enzymes; i.e.,
carbohydrases, lipases and proteases
Background
- Humans are composed of nonliving chemicals
- What do you think they are?
Main Molecules in Us
1 Carbohydrates
2 Lipids
3 Proteins
Carbohydrates
1. Carbohydrates
- Main job: provide us with fast source of energy
- They make up the largest part of our diets
- What are some examples of carbohydrates in your
diet?
- Why should we not have too much extra energy?
Carbohydrates Chemistry
- Carbohydrates have a single sugar unit or are polymers of
many sugar units
- Formula for single carbs have a 1:2:1 ratio of carbon to
hydrogen to oxygen
CnH2nOn
Carbohydrates Chemistry
- Scientifically naming a sugar depends on the number of carbons that are
in it
3C → tri- 5C → pent- 6C → hex-
- Sugars with more than 5 carbons will form rings
- Most carbs have the suffix –ose
- Common sugars are glucose found in the blood, sucrose found as sugar,
fructose found in plants, and deoxyribose found in DNA
A.Monosaccharides
1. Glucose
- Aka blood sugar
- The sugar required to make energy
- Problem: diabetes mellitus (too much blood sugar)
A.Monosaccharides
2. Fructose
- Fruit sugar
- Sweet type of monosaccharide
A.Monosaccharides
3. Galactose
- In pectin (thickens jams)
- Jello
- They are called isomers, what do you think an isomer is?

B. Disaccharides
They are a combination of two monosaccharides
Sucrose Maltose Lactose

- Milk sugar
- White table sugar - Malt sugar - Glucose +
- Glucose + fructose - Glucose + glucose galactose
- Extracted from sugar - Found in seeds of
beets or sugar cane germinating plants
B. Disaccharides
1. Joining monosaccharide molecules
- Called anabolic reaction
- It is through a process called dehydration synthesis
- When 2 monosaccharide molecules join together, they
lose a water molecule
Dehydration synthesis
Monosaccharide + monosaccharide → H2O + disaccharide
Glucose + Glucose → H2O + Maltose

B. Disaccharides
2. Breaking apart disaccharides
- Called catabolic reaction
- It’s done through a process called hydrolysis
- Adding a water molecules to divide the disaccharide
into 2 monosaccharides
Hydrolysis
C. Polysaccharides
1. Starch
- This is how plants store energy / sugar
- Two forms:
- Amalose (1000 or more glucose with 1 to 4 binding)
- Amylopectin (1000 - 6000 glucose with short branching chains of 24 to 36)
- Found in: foods, potatoes, pastas, rice.
- DOES NOT dissolve in water
- Digestible
StarchAmylase Maltose
Maltase
Glucose +
Glucose
C. Polysaccharides
2. Glycogen
- It is how WE store sugar –it’s storage polysaccharide
- Similar structure to amylopectin, except branches only 16-24 glucose
- Found in our muscles and liver
- Our body pulls it out of storage when our blood sugar (glucose) levels are
low
- The hormone glucagon turns stored glycogen into glucose
C. Polysaccharides
2. Glycogen
- The hormone insulin takes glucose out of the blood and into the cells
(for energy use)
- GLYCOGEN IS NOT FAT
- Glucose  Blood sugar
- Glycogen  Stored energy
- Fat  More storage (beyond glycogen)

C. Polysaccharides
3. Cellulose
- Makes up the cell wall
- 50% of all carbon is stuck in this form
- It doesn’t tend to form coiled structures like starch, but has more
layered structures
- Tends to have hydrogen bonds between OH groups
Lipids
Lipids
- Lipids are insoluble… why?
- Made of two structural units:
1. Glycerol
2. Fatty acid
- Like complex carbohydrates, they are made using dehydration
synthesis
Lipids
Main functions:
1. Storage of energy for long term
2. Key components of cell membranes
3. Act as a cushion for delicate organs of body
4. Serve as carriers for vitamin A, D, E and K
5. Raw material for the synthesis of hormones and other chemicals
6. Insulation
Lipids
Waxes
Phospholipids
Triglycerides
1. Triglycerides
- Formed from union of glycerol and three fatty acids
- Saturated fat: Solid at room temperature
- Unsaturated fat: Liquid at room temperature
- Oil
2. Phospholipids
- Phosphate group bonded to a glycerol backbone
- Have hydrophilic and hydrophobic ends
3. Waxes
- Long chain fatty acids joined to long chain alcohols or to carbon
rings
- Insoluble in water so good for waterproofing

Liposome Technology for Drug Delivery
- Lipids tend to assemble themselves into double layered spheres
the size of cells
- These are called liposomes
- They are able to fuse with cells to deliver contents to the cell
interior
- Currently used to fight cancer, delivering anti-cancer drugs
- Currently also used for gene therapy
Proteins
Proteins
- They form structural parts of cells
- They’re made of building blocks called amino acids
- R-groups change depending on different amino acids
Proteins
- Nearly everything is made of proteins
- Antibodies are a specialized type of proteins
- Proteins are different from carbs and lipids because they have
nitrogen and often sulfur
- They can be used for energy but it is not the main function of
proteins
Proteins
- Proteins allow for diversity
- There are 20 different amino acids that can be arranged in a
limitless amount of ways
- Also, proteins can be made up of as few as a couple of AA up to
more than 250000 AA
Amino Acids
Proteins
- The sequence of AA determines the protein
- So different sequences give us different proteins
- These sequences will be determined by your genes
Protein formation
1. Dehydration synthesis occurs where a H2O molecule is removed,
2. Then, a covalent bond forms between the carboxyl group of one
AA and the amino group of adjacent AA
- This is called a peptide bond
Proteins
- Polypeptides: chains of amino acids
- Your body can make many of the amino acids, but there are 8
that the body cannot make
- These 8 AA are called essential amino acids
How do you think you can get the essential amino acids?
Structure of Proteins
- Proteins are polypeptides that are folded into specific 3D shapes
- Some may contain more than one polypeptide
- The shape and structure of proteins determines their function
Four levels of structure
1. Primary: this is the unique sequence of amino acids
2. Secondary:
- Determined by the Primary structure and H-bonds between the amino
acids
- Two secondary structures: either AA chain coils or folds
3. Tertiary: Additional folding caused by the R-groups
- Example: Disulfide bridges
- Example: 1 hemoglobin around a single iron

4. Quaternary: larger globular proteins formed from two or more polypeptides
- Example: functional hemoglobin has 4 subunits

Denaturation and Coagulation
- Denaturation: disruption of bonds that change the configuration of the
protein
- Caused by excess heat, radiation, change in pH, etc.
- The protein may uncoil or assume a new shape, but once the “cause” is
removed, the protein may revert back to its original
Denaturation and Coagulation
HOWEVER
- If the change is permanent, then that is coagulation
Can you think of any permanent changes to proteins?

Practice
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Essential Nutrients

Chapter 8 - Digestive System

- They are called isomers, what do you think an isomer is?

Sucrose Maltose Lactose

Glucose + Glucose → H2O + Maltose

- Glucose  Blood sugar

- Glycogen  Stored energy

- Fat  More storage (beyond glycogen)

- Saturated fat: Solid at room temperature

- Unsaturated fat: Liquid at room temperature

- Have hydrophilic and hydrophobic ends

- Insoluble in water so good for waterproofing

3. Tertiary: Additional folding caused by the R-groups

- Example: Disulfide bridges

- Example: 1 hemoglobin around a single iron

4. Quaternary: larger globular proteins formed from two or more polypeptides

- Example: functional hemoglobin has 4 subunits

- Caused by excess heat, radiation, change in pH, etc.

- If the change is permanent, then that is coagulation

Can you think of any permanent changes to proteins?

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