WEEK2: NUTRITION PRINCIPLES - MACRONUTRIENTS

PROTEINS
Proteins are derived from the greek word Proteios' meaning of utmost importance or holding first
place . Proteins are complex forms of amino acids, where an amino acid is a simple organic compound containing both a carboxyl group (-COOH) and an amino ( -NH2) group.
Proteins are the major structural component of muscle and other tissues in the body. They are required
to produce hormones, enzymes and even haemoglobin.

USE OF PROTEINS IN THE BODY

Proteins come in many different forms and have many different functions in the body. They can be
divided broadly into static (i.e. structural) and dynamic functions:
Static: Certain protein performs brick and motor roles in the body and are primarily responsible for
structure and strength of the body. Collagen and elastin, both types of proteins, are found in the bone
matrix, vascular system and other organs and alpha keratin is another protein present in epidermal
tissues.
Proteins combine with nucleic acids to form nucleoproteins and are present in every cell of your body.
Your DNA dictates your protein synthesis sequence in the body which creates replacement cells and
tissues in the body. Bones are also mainly composed of proteins with calcium, magnesium and phosphate.
Dynamic: These functions are more diversified they include protein acting as enzymes, hormones,
blood clotting factors, genetic control, storage protein, muscle contraction, etc.
So protein plays a vital role in human body although the main aim of protein is not energy production
like its counterparts- carbohydrates and fats. But protein essentially helps in building and maintaining
muscle mass, and when required for metabolism as well. These roles are big and very important too.
Excess protein is either converted into energy, through the process of Gluconeogenesis, or converted
into fats.

DIGESTION AND METABOLSIM OF PROTEINS

Now that we know how important protein is to the body when it comes to recovery and growth, let us
delve into how body digests and metabolises protein.
The cells in the intestine cannot absorb whole proteins, they need to be broken down into small chains
of two or three amino acids first - called peptides.
This breakdown first starts in the stomach, where Hydrochloric Acid (HCL) and Pepsin begin protein
digestion by breaking down peptide bonds into simpler amino acids. Rennin is an enzyme that is
present in infants to help break down milk protein.
The pancreas releases digestive enzymes into the small intestine. In the first section of the small intestine, the duodenum, trypsin further breaks down proteins into single amino acids by a process called
hydrolysis.
Trypsin also activates the enzymes chymotrypsin, carboxypeptidase and elastase that are released into
the small intestine for amino acid chain breakdown.

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Fig 1: Enzymes and Hormones involved in Digestion of Proteins. Source: CNX

The process of breakdown of proteins is called proteolysis. The smaller peptides are absorbed from
the small intestines into the mucosa cells. Sodium and potassium are the minerals needed for the
amino acids to pass from the intestines through the villi and into the bloodstream.
The single molecule amino acids, or free amino acids, absorbed through the wall of the small intestine
are now used for the last part of protein metabolism, protein synthesis. The proteins ingested from
animal and plant protein sources are made into new tissues or used for tissue repairs in the body (hair,
skin, nails, muscle) or they are broken down and used for energy. If excess amino acids exist, the
body has no mechanism to store them and so they either get converted into glucose or ketones or decomposed into hydrocarbons and nitrogenous waste which is expelled out of the body through urea
cycle.
Processing of Amino Acids results in creation of metabolic intermediates which enter energy production through Krebs cycle.

TYPES OF PROTEINS
Amino acids can be divided into two types based on their synthesis in the body:
a. Essential amino acids: Human body cannot synthesise these amino acids and so they need
be a part of the diet.
b. Non-Essential amino acids: Nonessential effectively means that our body can make them
and so their dietary requirement is not essential.
The essential amino acids are: Phenyl alanine
Valine
Tryptophan
Threonine
Isoleucine

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Methionine
Lysine
Leucine

Protein from animal sources generally have a complete amino acid profile. i.e. in relation to the human bodys need for essential amino acids. Foods like meat, fish, eggs and dairy have a good amino
acid profile and regarded as high quality proteins.
Vegetarian sources of proteins are also perfectly good sources of proteins and complete amino acid
profiles can be obtained from these by consuming them in combinations. One example of such combination is rice and beans where most beans are low in methionine and high in lysine while rice is low
in lysine and high in methionine.
Some exceptions to vegetarian sources of protein, which have a complete amino acid profile are
Quinoa, Soy and its related products like Tofu, Tempeh, etc.
QUALITY OF PROTEINS
Protein Efficiency Ratio (PER) is the simplest measure of the quality of a protein. It represents the
gain in body weight in grams to gram of protein ingested during a test period. PER for egg is 4.5, for
milk protein is 3.0 and rice protein is 2.2
Biological Value (BV): is a measure of how efficiently the body utilises the protein absorbed from the
diet. Higher the value, better it is. It takes into account the nitrogen used for tissue formation and to
what levels nitrogen is absorbed via food. This is then multiplied by 100 to express it in form of a
percentage.
Even though BV is a reasonably good index for assessing the Its limiting factor is that it only looks at
protein efficiency from the point that it is available to the body, i.e. only the digested protein. NPU
overcomes this limitation.
Net Protein Utilisation (NPU) is similar to BV but slightly better since it takes into account the digestibility factor. Both measure the same parameter of nitrogen retention where the basic difference
lies in that the BV is calculated from nitrogen absorbed whereas NPU is from nitrogen ingested.
Another not so popular measure is a Chemical Score. It rates the amino acid profile of the limiting
essential amino acid with a reference protein (like egg).

Source: Ternopil State Medical University

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Finally, the Protein Digestibility Corrected Amino Acid Score (or PDCAAS) rating was adopted by
FDA and FAO as the preferred best method to measure quality of protein. It is similar to Chemical
Score except in PDCAAS, the chemical score is adjusted for true fecal digestibility of the test protein.
To know more about PDCAAS, its advantages and disadvantes, you can read through these links here
and here.
The criticism of these values has been that the numbers were obtained by tests done on rats and might
not be directly applicable to humans. Further, the rats were fed a diet which consisted of 10% protein
after being deprived of proteins for the 10 days leading up to the start of the test. We can see many
problems with this, but these are the only standardised and most widely accepted measure of quality
of proteins we have till date.

SOURCES FOR PROTEIN

Healthy sources of dietary proteins includes lean cuts of beef, fish, eggs, legumes and dairy products
like milk, cheese, yogurt, etc.
Protein is also present in smaller quantities in starchy foods and vegetables.

PROTEIN INTAKE:
The suggested intake of protein is roughly 30-35% of the overall calories. The current RDA for all
adults for protein is at 0.8g/kg. This needs to be revised upwards in case of those involved in sports or
any physical exercise. The optimal intake for those practising strength training and in need to gain
muscle mass has been determined to be 1.8g /kg /day. Read more about this in a detailed review of
various studies in this article.

An excerpt from a popular study which summarises the researches thus far on protein intake confirms
that the RDA for an endurance athlete is closer to 1.3g /kg /day while for a strength athlete it is closer
to 1.8g /kg /day.
In case of an obese person, this needs to be reduced and should be calculated basis lean body mass.
SOME KEY AMINO ACIDS
Out of the eight Essential Amino Acids, three are called branched chain amino acids (BCAA). These
are Leucine, Iso leucine and Valine. Out of these three, Leucine is mainly responsible for muscle protein synthesis (or MPS i.e. building and maintaining muscles). This BCAA simulates a protein known as mTOR, which is very important for muscle growth. The amount of leucine required to give
this signalling effect and start MPS is higher than its requirement in the actual muscle building

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process. Excess leucine will be oxidised and eliminated once it has done its signalling work. This is
fine and has no adverse effect of any kind.
In effect the amount of leucine concentration in the food determines the optimal amount of protein for
muscle building per meal. It is understandable then that of all the protein sources, foods containing
leucine are quite effective in stimulating muscle protein synthesis.
The key is to remember that not just taking a particular quantity of protein is important but at the
same time care has to be taken that 2.2 to 3.0 grams of leucine is consumed in every meal, this will
ensure maximum MPS. If you consume 10g of essential amino acids (from complete protein sources)
in any meal, this requirement of leucine is covered and you would not require additional leucine supplementation (Ref2). In order to get maximum utilisation of protein towards muscle building it is
therefore recommended that proteins with complete amino profiles (or those high in leucine) should
be consumed as part of all meals.
Iso leucine- is also responsible for MPS and is more effective than Valine but weaker than Leucine. It
helps in mediating glucose uptake in the cell and break it down into energy as compared to other
amino acids. The recommended dosage for a 150lb person is 3.3-4.9.
Valine: deficiency of valine can cause fatty liver formation. It reduces the fractional clearance rate of
glucose.
Alanine: It enhances muscular endurance. Basically it helps in adding one to two additional reps in
the gym. When it is taken it turns to Carnosine (another protein - a dipeptide of beta-alanine and histidine), which acts like an acid buffer in the body. It is released in response to drop in pH. Increasing
stores of Carnosine can protect from drop in pH which is diet induced (ketogenic diet) or from exercise induced lactic acid production.
Glutamine: It is found in the skeletal muscle and other muscle fibres. It is an effective intestinal and
immune system health compound.
Arginine: This amino acid directly produces nitric oxide via the nitric oxide synthase enzyme.
Citrulline: This gets converted into arginine in the kidneys. The absorption rate is better than arginine
and it can raise the plasma arginine levels of arginine more effectively than arginine itself.

ISSUES WITH PROTEIN CONSUMPTION

DEHYDRATION AND CONSTIPATION: Diets which are very high in protein are largely constituted
by replacing the fibre content in a meal. Very high protein diets followed by most muscle building
enthusiasts, can lead to constipation. Further, to flush out the ammonium ions produced during protein
breakdown, in case of excess protein, the body might need to urinate more frequently which can cause
dehydration to set in as well.
GOUT: is a condition which develops when the level of uric acid becomes high in the body. It leads to
formation of crystals that accumulate around a joint. For centuries, Gout has been associated with
over consumption of meats, seafoods and alcohol. Even though the real cause, as to why it inflicts
only a certain population and not others, is still unknown, it happens in people who have a genetic
disposition to uric acid accumulation and crystal formation (Ref3).
KIDNEY DISEASES: For someone whose kidney is already impaired, a high protein diet can cause
further stress to their system. High protein diets like Atkins, are not recommended for those with
semi-functional kidneys.

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References:
Ref1: Complete source of proteins for vegetarians: http://greatist.com/health/complete-vegetarian-proteins
Ref2: Excess Leucine enhances Muscle Anabolic Signalling but not net Protein Anabolism: http://
jn.nutrition.org/content/140/11/1970.full
Ref3:Gout linked genetic mutation leads to diseases: http://www.news-medical.net/news/20130409/
Johns-Hopkins-researchers-find-how-gout-linked-genetic-mutation-contributes-to-disease.aspx

Recommended Reading
1. Protein metabolism and digestion: http://osp.mans.edu.eg/medbiochem_mi/Cources/Biochemistry/
2nd_year_medicine/Protein_metabolism/files/Lecture_01.htm
2. Nutrient Timing Endures: Circadian Rhythm Protein Timing: http://www.humanengine.com/index.php/articles/nutrition/item/nutrient-timing-endures-circadian-rhythm-protein-timing?category_id=3

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