Module 5

Lecture 01
 Panacea: a term for “cure all”, like protein can help you gain and lose weight.
 Average woman gets 35% MORE protein than their DRI and men 65%.
 Elderly women are at risk of not getting enough protein.
 Daily value is the percentage of the nutrient that meets the needs of the population that
needs it the most, and that is teenager boys.
 Remember: animal foods have no fiber.

 What is protein:
 Component of every living cell.
 Made up of amino acids.
 Of the 20 amino acids, 9 are essential and can’t be made by the body.
 We need enough protein to make the 11 nonessential amino acids.
 Amino acids are connected by peptide bonds.
 All amino acids contain Nitrogen, proteins are 16% nitrogen by weight.
 Protein intake (g) = nitrogen intake (g) x 6.25 (6.25 is 1 over 16%)
 We lose nitrogen through urine.

 Amino acids
 Every amino acid has a central carbon
 It has a hydrogen, acid group, and an amino group
 The side chain is what makes an amino acid unique
 Ex: glycine has a side chain that is one Hydrogen
 Ex: methionine has a side chain of CH2-CH2-Sulfur-CH3
 Ex: phenylalanine has a side chain of CH2-ring structure
 Phenylalanine is found in aspartame, an artificial sweetener. The ring structure is what
makes it sweet.
 PKL: inability to break down extra phenylalanine. It causes brain damage because of
accumulation. They can’t consume anything with artificial sweeteners.


 Normal metabolism breaks phenylaniline into tyrosine.

 Memorize essential amino acids on table 6.1
 Protein structure:
 When two amino acids join, they lose a water and form a peptide bond.
 Now we have a dipeptide.
 How many peptide bonds in a tripeptide? 2 peptide bonds.
 Protein primary structure: linear order of amino acids as predicted by DNA.
 Secondary structure: some side groups have charges, or are hydrophobic, causes the
structure to change shape. They either are helixes or beta sheets.

 Tertiary structure: helixes and beta sheets fold on each other forming a 3D shape.

 Protein structure and function:

 Amino acid sequence of a protein determines its final 3D shape.
 A protein’s 3D shape is critical for its function.
 Ex: insulin is a protein. Not all hormones are proteins, but insulin is.
 Insulin is made of 2 polypeptide chains.
 An amino acid with a sulfur group on each polypeptide join and form a disulfide bridge.
There are 3 bridges.
 When comparing cow, pig, and human insulin the sequence was identical except for 3
different amino acids.
 It is the order of amino acids that dictate the shape of insulin.
 Denaturation: ruin the 3D structure of a protein by acids, bases, or heat.
 An enzyme is a protein; if we eat protein will be denatured in the stomach.
 Altering amino acid sequence can change protein function dramatically.
 Ex: hemoglobin is how we transport oxygen; it is a blood protein.
 Iron in at the center of each hemoglobin amino acid. 4 hemoglobin amino acids join to
form a hemoglobin molecule, so there are 4 iron centers.
 1 amino acid change can cause sickle cell anemia.
 Anemia does not mean lack of iron; it is reduced oxygen carrying capacity of the blood.
 What happens in hemoglobin protein in sickle cell anemia:
 Change in an amino acid changes the shape of the protein  red blood cell

 What foods provide most protein?

 Cruciferous vegetables include broccoli, cauliflower, kale, Brussel sprouts, have higher
protein than other vegetables.
 Fish has lots of protein, but the population does not eat enough fish so our intake of
protein from fish is low.
 Grain products provide the most of our protein from our diet.
 Grain, milk products, and meats provide the most of our protein intake.
 Meat and alternatives are the highest protein sources, and then milk products.
 Why do we need proteins?
1- Regulatory proteins: regulate body processes
 Ex: some hormones like insulin, glucagon.
 Enzymes like trypsin that digests protein, lipase, amylase. All enzymes are protein.
 Neurotransmitters which are signaling molecules for the brain like serotonin.
2- Growth and repair for tissues:
 Muscle protein like collagen; supports the skin and bone.
 Eating collagen does not pass through the stomach and does not go to the specific
areas. It is broken down to the amino acids and the body sends them to specific body
parts.
 Actin and myosin work for muscle contraction and relaxation.
 Normal “turnover”: breakdown and replacement of body tissues and increases when
bones are broken.
 More protein synthesis would be going to that area.
3- Immune defense:
 Antibodies are proteins that fight invading microbes
 Transportation like hemoglobin transporting oxygen
 Transferrin is a protein that transports iron.
4- Energy:
 True that all consumed proteins may be digested and resulting amino acids can be used
for kcal.
 But body cells prefer energy from fat and glucose.
 Carbs and fats cannot do any of the other protein roles, so the body prefers using the
amino acids for the other roles rather than energy.
 Amino acids must be turned to glucose  lose kcal

 Protein digestion and absorption: red = active enzyme

 Protein enters the stomach first.
 Carbs and fats are not digested in the stomach, but protein is.
 HCl denatures the protein, so the protein’s function is gone.
 Now that the 3D structure is gone the peptide bonds are accessible.
 Pepsin is an enzyme that breaks the peptide bonds, and the protein becomes small
chains of peptides.
 Now the pancreas releases pancreatic pre-enzymes.
 They’re not active enzymes, otherwise the pancreas would digest itself.
 The pancreas releases trypsinogen and chymotrypsinogen into the small intestine.
 Now the intestine creates intestinal enterokinase.
 It will act on trypsinogen and convert it to trypsin.
 Trypsin activates various intestinal pre-peptidases.
 Trypsin converts chymotrysinogen  chymotrypsin.
 Trypsin cleaves peptides into smaller peptides.
 So now all the peptides are broken down to amino acids + di- and tripeptides.
 Mucosal cells absorb di and tri peptides better than amino acids.
 So amino acid supplements do not help with absorption.
  Once di and tripeptides are absorbed into mucosal cells, they’re broken down to
individual amino acids.
 So, when they enter the portal system, we have individual amino acids into the blood.
 The blood always goes to the liver first for detoxification.

 Amino acids in liver:

 Amino acids  portal vein  Liver
 Liver synthesises amino acids into required body protein.
 Ex: if you’re fighting infection, it would turn them to antibodies.
 If the body is starved, the amino acids are instantly used as energy for liver cells.
 Amino acids are converted to glycogen if other body cells are starved.
 Excess amino acids are converted to fats and sent out through VLDLs to adipose tissues.
 Figure 6.8.

 Overall amino acid metabolism scheme:

 Every cell has an amino acid pool.
 We cannot store protein; we store it for around 30-40 minutes.
 What feeds the amino acid pool is amino acids from our diet (exogenous tissue) or from
body tissue breakdown (endogenous source).
 The body would synthesize body proteins, but lean body mass is only created if the
person is exercising.
 Whatever excess amino acids that are not used are NOT stored; they are broken down
by deamination.
 Deamination: the amino group is removed as free ammonia, which is toxic to the body,
so it is converted to urea in the liver  urea to kidney  urea in urine  exited from
body.
 The rest of the amino molecule is called the carbon skeleton.
 It can be:
1- Used directly by cells as kcal if there is not enough kcal in the body.
2- Carbon skeleton is converted to glucose if the body does not have enough carbs in the
diet  gluconeogenesis.
3- converted to fat  stored in adipose tissue.

Lecture 02

 protein quality:
 quality of a protein is determined by:
 digestibility of a protein.
 Types of amino acids.
 Proportion of amino acids (in comparison to gold standard protein source like chicken
egg, breastmilk).
 Plant proteins always have lower digestibility because of the fiber in the plants.
 What is a good quality protein:
 Well (completely digested).
 Ex: animal proteins (90-99% digestion), plant proteins (70-90%), legumes and especially
legumes (more than 90%).
 Contains all the essential amino acids and proportions like the body’s requirements.
 AA reference is mg AA/g of total protein.
 Lysine: 51 mg AA/g protein
 Methionine +cysteine: 25 mg AA/g protein
 Egg has 70 lysine and 57 methionine +cysteine; has more than needed which makes it a
golden source.
 All legumes are short on sulfur amino acids (methionine + cysteine).
 The limiting amino acid for legumes then is methionine cysteine.
 That’s why all plant sources are incomplete protein sources.
 When combining a legume and grain, we get all the required AA.
 Limiting AA in grains is lysine.

 Protein quality from different foods:

 Animal foods will always be complete protein sources.
 Ex: fish, eggs, dairy, poultry, meat.
 Proteins from plant foods will lack at least 1 essential AA.
 Soybeans will be closest to animal proteins but still lack some AA.
 International theme: grains + legumes + seeds + nuts
 Assigned reading: what are potential benefits of plant diets + which nutrients are at
insufficient intake in a poorly planned vegetarian diet? No measuring protein quality
DIAAS%.

 How much protein do we need?

Protein Nitrogen balance Examples
Nitrogen coming in Zero nitrogen balance Any adult maintaining their
(protein) does not equal weight
nitrogen common out
(urine, fecal, skin, sweat).
Nitrogen in > nitrogen out Positive nitrogen balance Gaining body weight or
repairing body tissue.
Infant, child, adolescents,
pregnancy, broken bones,
athletic training (but only if
additional lean body mass
is being gained).
Nitrogen in < nitrogen out Negative nitrogen balance Losing body weight.
Dieting, wasting
(starvation), disease
(burns), extreme inactivity
 or weightlessness
(astronaut).

 DRI Values of protein:

 ADMR (DRI): 10-35% kcal
 RDA Value: adults (19 and older) need 0.8g/kg of body weight/day
 Protein requirements are the highest in infancy, then they start decreasing.
 how much protein did I eat yesterday?
1- Determine personal protein requirements.
I’m 125lbs  2 lbs = 1kg  56.8 kg
56.8kg x 0.8 = 45.5g of protein per day

 What we need vs what we eat:

 Canadians consume 15% kcal from protein.
 The DRI AMDR intake is 10%-35% kcal
 Most people in north America eat twice the amount of protein they need.
 Do athletes need more protein than non-athletes? YES.
Individual Protein requirements
Non-athlete 0.8
Endurance athlete 1.2-1.4
Power athlete 1.2-1.7
 Calculations:
 Average jane: she is 60kg (x2.2 = 132lbs) and has 2000 kcal per day and 15% of her kcal
comes from kcal.
1- 15% x 2000 = 300 kcal. 4kcal per 1 g of protein  300 / 4  75 g protein.
2- 75g/60kg  1.25g/kg/per day which is over the 0.8.
 Athlete jane: she is 60kg and eats 3000 kcal and 15% of her kcal come from protein.
1- 15% x 3000 = 450 kcal / 4 = 112 g protein
2- 112g/60kg = 1.9g/kg/day which is even more than a power athlete.

 Amino acid supplements:

1- Absorption and transport issues:
 At the GI tract, amino acids share transporters and compete for absorption in the GI
tract.
 Ex: phe, trp, and tyr share a transporter.
 If a person takes a trp supplement, you overwhelm the transporters with one amino
acid and prevent the others from absorption.
2- Brain has a blood brain barrier: before the blood gets to the brain there’s a barrier
that has transporters to pick up combinations of amino acids.
 If we take too much tryp, we overwhelm the transporters and neglect other amino acids
from being absorbed.
 Tryp is used to make serotonin.
 If you take more phe, less tryp would get absorbed, which means less serotonin  bad
mood
 Risk: AA imbalances and mood changes.
 N-retention: how much nitrogen do you keep in the body after eating protein?
 The amount of nitrogen kept following eating protein is more than following eating free
amino acid supplements.
 Bottomline: get your protein from food.

 Is too much protein bad?

1- More protein increases calorie intake  overweight.
2- High protein foods tend to be high in fat (pizza, steak, hamburgers).
3- Causes more calcium loss in urine. People who don’t get enough protein have problems
in their bone health, so we need adequate protein. But high intake of animal base
protein is high in sulfur containing AA, and when they are metabolised, they’re turned
to an acid group, so it draws calcium out of the bone to neutralize the acidity. If the
animal protein is eaten with plants or a glass of milk, the effect is negated.
4- Overworked liver and kidney ONLY IF you are at risk of liver or kidney problems.
5- Excess protein does not cause cancer, but diets higher in red or processed meats are
associated with higher risk of cancer.
6- Excess protein might impact gut microbes (new research).