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 THE BSY GROUP

NUTRITION COURSE – THE SCIENTIFIC APPROACH

LESSON THREE
 THE BSY GROUP

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 THE BSY GROUP

NUTRITION COURSE – THE SCIENTIFIC APPROACH

LESSON THREE

LEARNING OUTCOMES

On completing the study of this lesson you should be able to:

1) Summarise the different types of carbohydrates and their dietary sources

2) Demonstrate knowledge of the amino acids required by the body and how these
combine to form proteins

3) Assess the differences between the various lipids present in food and their effects
on cellular function

4) Evaluate the sources, functions and symptoms of deficiency of the water-soluble

vitamins
 THE BSY GROUP

NUTRITION COURSE – THE SCIENTIFIC APPROACH

LESSON THREE

ESSENTIAL NUTRIENTS

As has been mentioned in Lesson One, the essential nutrients that make our body grow
and function are carbohydrates, proteins, fats, vitamins and minerals. This lesson and
Lesson Four will be about knowing what these are and what they do once in the body, as
well as what the symptoms and disorders that deficiency of any of the nutrients can lead
to.

Carbohydrates
Carbohydrates (CHO), found mainly in grains, starches, vegetables and simple sugars, are
the major source of human energy. They are composed of carbon, hydrogen and oxygen
in the ratio of 1:2:1. Glucose is the main fuel used by all the organs and carbohydrates
and some proteins are converted into glucose for the body to use. A deficiency of
carbohydrates, which can happen in low carbohydrate diets or starvation, leads to
accumulation of ketone bodies (ketosis). Ketosis can cause a disturbance in the body’s
acid base balance, forming more organic acids. This can cause bigger problems over
longer periods, even though in a time of starvation, ketones are used by the brain and
muscle for energy. The three main types of carbohydrates are monosaccharides,
oligosaccarides and polysaccharides.

 Monosaccharides are the simplest form of carbohydrates, and they cannot be

reduced in size by hydrolysis. Most monosaccharides are made of six carbons or
hexoses (hex = six, ose = ending for all sugars).

Glucose can be found in two isometric forms (steroisomers), D-glucose and L-

glucose. D-glucose is the only one that is used in the body. Sources of glucose are:
 Nutrition Course – The Scientific Approach: Lesson Three

honey, sugary foods, fruit and fruit juices, vegetables and ice-cream. Glucose is
the major sugar used by many organs as fuel, including the brain, and for this
reason its level needs to be controlled within narrow limits by a number of
hormones (e.g. insulin and glucagon). Fructose is metabolised by the liver into
glucose, glycogen, lactic acid and fat. Galactose is found in fermented milk, and it
is used by the nerve tissue in growing infants and metabolised into glucose
and/or glycogen for storage. Other monosaccharides include xylose, arabinose (in
white wine and beer), mannose (in fruit) and fucose, found in human milk and
bran. Sugar alcohols (xylitol, sorbitol and mannitol) are nutritionally important, as
they are metabolised into glucose slower than the other simple sugars, which can
be used in hypoglycaemic disorders and/or by diabetic people.

 Oligosaccharides are made of short chains of monosaccharide units joined by

covalent bonds (sharing of electrons between atoms). The most abundant
oligosaccharides are made of two monosaccharide units (disaccharides): sucrose
(found in cane sugar and beet sugar), lactose (found in milk and milk products)
and maltose (found in beer and malt liquors). Other oligosaccharides such as
galactosyl-sucroses, found in legumes and fructosyl-sucroses, found in onions,
leeks and artichokes are resistant to digestion in the upper gastrointestinal tract
and reach the colon unchanged. Here fermentation by the good bacteria occurs,
forming by-products, such as volatile fatty acids and gases, which can lead to
flatulence. In order to be absorbed and utilised by the body, oligosaccharides and
disaccharides need to be hydrolysed into their monosaccharide units by their
specific enzymes. Hydrolytic enzymes are called carbohydrases (ase = word for
ending enzymes). The enzymes that break the disaccharides into monosaccharides
are:

Sucrase = sucrose into fructose and glucose

Lactase = lactose into galactose and glucose
Maltase = maltose into two glucose molecules

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 Polysaccharides are made up of long chains of monosaccharide units that might

go from several numbers into hundreds or thousands. The polysaccharides can be
divided into digestible and indigestible polysaccharides. The starches are the most
digestible polysaccharides, and are found mostly in plants. Amylase and
amylopectin are the main two forms of starches and are made of polymers of D-
glucose. Starches are found in cereals, grains, potatoes, legumes and other
vegetables.

The digestion of starches starts in the mouth with the alpha-amylase enzyme,
found in the saliva. It continues in the stomach until there is a breakdown of the
polysaccharides into short chain polysaccharides (dextrins) and maltose. There is
no digestion of dextrins and disaccharides in the stomach. Further digestion by
the enzymes is made in the microvilli of the upper small intestine by the alpha
amylase secreted by the pancreas with the maltase, isomaltase, sucrase and lactase.
Once the digestible polysaccharides are broken down into their simple sugars,
they are absorbed through the small intestine into the bloodstream for their use.

Non-starch polysaccharides (NSPs) are the components of plant walls, and are
mostly not digested by humans. NSPs are divided into cellulose and non-
cellulosic polysaccharides. NSPs are made of a number of polymers of simple
sugars, together with uronic acid. Cellulose is the main component of cell walls in
plants and they are mostly insoluble, although an increase of uronic acids
increases their solubility. For example, whole grains and wheat bran contain a
high amount of NSPs and only traces of uronic acids, making them insoluble, but
oats and barley contain a good source of beta-glucans and therefore are more
soluble. Fruits and vegetables, on the other hand, have more uronic acids and
pectin in their NSPs, which makes them more digestible.

Non-cellulosic polysaccharides are the hemicelluloses, pectins, beta-glyucans,

gums and mucilages. Mucilages (from seaweeds) and gums (from acacia tree) are
usually used by the food industry as thickeners, stabilisers and emulsifiers.

NSPs are generally considered to be dietary fibre, which does not provide much
energy for the body, but is a source of energy for the intestinal bacteria. Dietary

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fibre for this reason is considered an important part of healthy eating, as a good
healthy balance of intestinal bacteria will result in a decrease and/or prevention of
intestinal and colonic disorders. An intake of about 20 to 50 mg a day of dietary
fibre is recommended, which means at least five to ten servings of fruits and
vegetables a day, and two to three servings of whole grains and/or legumes.

Glycogen is the form in which carbohydrates are stored in animal tissues and
humans and it is mainly found in the liver and skeletal muscles. Glycogenolysis,
which is the process from which glycogen is metabolised into glucose, will be
discussed in Lesson Five.

Proteins
In Greek, protein means ‘taking first place’ or ‘primary’, which states their importance in
the body. Each protein is different and each of them is made up from the same 20 amino
acids. What makes the proteins different from each other is the sequence and number of
amino acids. There are over three million ways of arranging amino acids in the first five
places of a chain alone. Enzymes, hormones, structural proteins, immunoproteins and
transport proteins are all derived from proteins and amino acids. The formation of the
protein is controlled by the genetic make-up of our cells, encoded in DNA
(deoxyribonucleic acid) and RNA (ribonucleic acid) chains.

Proteins are found in both plants and animals. Once proteins are ingested they are
broken down into their basic amino acids and rebuilt according to our body’s needs. The
basic structure of protein is composed of an alpha carbon, a hydrogen atom, oxygen,
nitrogen and a part of a sulphur group. Amino acids have a hydrogen (H) atom and three
functional groups such as an amino group, and acidic carboxyl group and a side chain ‘R’
group, which changes with each amino acid. A peptide bond is a covalent bond between
one amino group and an acid group or carboxyl group of amino acids. A dipeptide is two
amino acids joined together, while a polypeptide is more than two amino acids joined
together. A typical protein can contain 500 or many more amino acids joined together by
peptide bonds.

Proteins are not just composed of long chains of amino acids, they are a complex three-
dimensional pattern. There are four different protein structures: primary, secondary,

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tertiary and quaternary. Primary structure is a unique sequence of amino acids linked by
covalent peptide bonds forming a polypeptide bond; secondary structure is a repeated
twisting or folding of neighbouring amino acids in the polypeptide chain; tertiary
structure is a three-dimensional shape of polypeptide chains, with several types of bonds,
the strongest of which is the disulfide bridge (sulphur bond); and the quaternary structure
is formed by two or more polypeptide chains.

The different structures and bonds are due to the fact that some amino acids are attracted
to other amino acids in the chain, while others are repulsed. This is possible due to the
side chain ‘R’ being different in each of them; they can have a negative, positive or neutral
charge.

The amino acids that proteins are made of are divided into essential and non-essential
amino acids. There are ten essential amino acids that need to be included in the diet, as
the body cannot make them. The non-essential amino acids can become essential in the
case of organ failures or inborn errors of amino acid metabolism. An example of inborn
error is phenylketonuria (PKU), where there is no phenylalanine hydroxilase activity
which hydrolyses phenylalanine to tyrosine, therefore tyrosine needs to be supplied
completely by the diet. Some amino acids can be converted into other amino acids, such
as tryptophan into serotonin, lysine and methionine into carnitine, tyrosine and
phenylalanine into adrenaline, noradrenaline, tyrosine and dopamine.

The essential amino acids are arginine (required only by growing children), histidine,
isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine.
The non-essential amino acids are alanine, asparigine, aspartic acid, cysteine, glutamic
acid, glutamine, glycine, proline, serine and tyrosine. A complete food is the one that
includes all of the nine essential amino acids. Animal protein such as meat, fish, dairy
and poultry are complete foods, while plant foods, such as grains, legumes, fruits and
vegetables are not considered complete foods when eaten separately. This is one of the
reasons for eating a variety of foods during the day, especially for vegetarian and vegans.
Whey protein (isolate) is a complete protein as it has all the essential and non-essential
amino acids. This is a good form of protein in case of muscle waste from a strict diet, old
age, recovery from surgery or other major disease.

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Digestion of protein begins in the stomach, where hydrochloric acid (HCL) denatures the
protein structures and begins the activation of pepsinogen to pepsin, which will further
break down the protein structure by breaking the peptide bonds. Protein will be broken
down in the stomach into polypeptides and oligopeptides and some free amino acids.
These will be fully digested in the small intestine by enzymes released by the pancreas,
before being absorbed into the blood stream.

Lipids (Fats)
Lipids (lip = fat) are nowadays one of the most talked about food groups and they mostly
have a bad reputation. But lipids make up a quarter of the body mass in a healthy, lean
adult and they are essential for a variety of structural and body functions. Lipids, unlike
carbohydrates, which are hydrophilic, are repulsed by water (hydrophobic) and therefore
little fat is dissolved in watery blood plasma. In order to be more soluble in water and
therefore carried to their target tissue, lipids need to join with hydrophilic protein
molecules and become lipoproteins. Lipoproteins transport lipids around the blood and
to the target tissues as well as removing them from the blood.

The body uses different types of lipids, the main ones being fatty acids, triglycerides,
phospholipids, steroids, bile salts, eicosanoids and leukotrienes. Fatty acids synthesise
triglycerides and phospholipids and they can be catabolised to make adenosine tri-
phosphate (ADP, energy production). Triglycerides are the most used lipids in the body
and they provide insulation, protection and energy storage; they can be solid, at room
temperature, or liquid (oil). Triglycerides include saturated fats, monounsaturated fats
and polyunsaturated fats. Phospholipids are the major lipid component of cell
membranes. Steroids include cholesterol as a precursor of bile salts, vitamin D and
steroid hormones, as well as being part of the cell membrane. Bile salts are needed for
digestion and absorption of fats. Eicosanoids and leukotrienes are both major
contributors to the inflammatory response and allergic reactions. Their function is to
respond to the stimulus of hormones, blood clotting, inflammation, immunity, stomach
acid secretion, airway diameter, lipid breakdown and smooth muscle contraction.

Lipids contain hydrogen, carbon and oxygen. The backbone of a lipid is a chain of carbon
atoms. Hydrogen and oxygen atoms attach to the carbon and form either a saturated fat,
where all available bonding sites are taken by another atom, or unsaturated fats where

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one or more bonding sites are free. When there are free bonding sites, the neighbouring
carbon atoms will form a double bonding. A lipid molecule with one double bond is
called monounsaturated fat (mono = one) and with many double bonds is a
polyunsaturated fat (poly = many). The unsaturated fat that contains the first double
bond at the third carbon is called an omega 3 fatty acid. If the first double bond is at the
sixth carbon, it is an omega 6 fatty acid and at the ninth carbon it is called an omega 9.

With the double bond, there are two forms of geometric isomerism – cis and trans –
which according to the form, can affect the properties of the fatty acid. The most common
natural found form is the cis isomers, where the hydrogen atom is on the same side of the
double bond. In the trans isomers, the hydrogen is on the opposite site of the double
bond which makes the molecule remain elongated and similar to the saturated fatty acids
but harder. Trans-fatty acids are mainly found in margarine, pastries, biscuits, and meat
products from cows and sheep. Margarine is made by adding a hydrogen molecule to the
unsaturated fatty acids, which will turn it unnaturally saturated and solid at room
temperature.

The alpha linolenic acids (omega 3) and linolenic acids (omega 6) are essential fats that
need to be included in the diet as our body does not make them. Saturated fats are found
in dairy products, a few plants such as cocoa butter, palm oil and coconut oil, meat and
meat products. Unsaturated fats are found in seeds, nuts, some plants such as seaweeds,
and oily fish. The body will make other oils from the essential oils and only a specific oil
from each of them. For example, from omega 3 the body will make eicosapentaenoic acid
(EPA) and docosahexaenoic acid (DHA), which can also be found in oily fish such as
halibut, salmon, mackerel, sardines, etc. From EPA and DHA the body will make type 3
prostaglandins which are anti-inflammatory, and fewer of the inflammatory leukotrienes.
This conversion can be much more efficient if EPA and DHA are supplied from the diet.
From the omega 6 oils the body can only make gamma linolenic acid (GLA), dihomo-
gamma linolenic acid (DHGLA) and arachidonic acid (AA).

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The following is the prostaglandins metabolism scheme:

 Omega 6
Linolenic acid Delta 6 desaturase enzyme (needs B6, magnesium, zinc and
it is inhibited by trans-fatty acids, saturated fats and
alcohol).
GLA Elongase enzyme.
DHGLA Delta 5 desaturase enzyme (needs vitamin C, niacin and
zinc).
Prostaglandins series 1 (PG1) (anti-inflammatory).
AA Delta 5 desaturase enzyme.
Prostaglandins series 2 (PG2) – (Inflammatory PGS) leading
to an increased inflammation with high AA in diet.
Enzymes involved in the making of the PG2 are cyclo-
oxygenase (COX) and lypoxygenase (LO).

 Omega 3
Alpha-linolenic acid Delta 6 desaturase enzyme.
EPA Elongase enzyme.
Prostaglandins series 3 (PG3) – EPA uses the same enzymes
of the AA to make the less inflammatory PG3, therefore
reducing the inflammatory cascades due to high AA in the
diet.
DHA Delta 5 desaturase enzyme

The above scheme shows that there is a competition between the oils for their enzyme use
and therefore the highest one in the diet will lead to a reduction of the other one’s end
product.

Each body cell has a permeable membrane. The membrane is made of cholesterol, fats in
the form of phospholipids (e.g. phosphatidylcholine) and proteins. The type of fatty acid
that the membrane has depends on the type of fat that is mostly consumed in the diet. For
example, a diet that is high in cholesterol and saturated fats, and/or trans-fatty acid
products, will result in the cell membranes being less fluid in nature than the cell

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membrane found in a person with a diet that has more of the unsaturated fatty acids.
This is an important fact, as the cell will be less permeable and more resistant to the
molecules that carry nutrients into the cell, resulting in cell starvation and disruption (e.g.
insulin resistance).

Cholesterol is as important as the other lipids; it is part of hormones, bile acids, sex
hormones, vitamin D and the cell membrane. It is found mainly in animal foods such as
meats, egg yolk, dairy products and shellfish such as prawns. The liver is the organ that
makes the most cholesterol, but an intake of excess cholesterol can be the cause also of
high blood cholesterol. Very low density lipoproteins (VLDL), low density lipoproteins
(LDL) and high density lipoproteins (HDL) are the complex lipotroteins/molecules that
transport blood cholesterol around the body. HDL is responsible for returning fats from
the blood to the liver to be used as energy or to be eliminated, while VLDL or LDL are
responsible for delivery from the liver to the body cells. High VLDL or LDL is associated
with the high cholesterol which can cause heart problems, while high HDL is associated
with reducing heart disease. Higher intake of omega 3 seems to be inversely related to
heart disease, but the important factor for prevention of cardiovascular disorders is
especially the ratio between LDL/HDL, where HDL should be higher than LDL.

Lipase is the enzyme that breaks down the various fatty acids and fat molecules. Fat
digestion mainly starts in the stomach, where fats are turned into emulsion. The main fat
digestion is done in the small intestine, and lipase, secreted by the pancreas, is the main
enzyme that splits fats into a mixture of fatty acids, glycerol and monoglycerides. As
lipids are not water-soluble, they are further broken down into their components of
fat-soluble and water-soluble droplets by the bile acids. Micelles are the result of the split,
which diffuse easily into the intestinal cells. The fat-soluble part is then attached to
chylomicrons (lipoproteins), and carried to the liver and other tissues, where the
lipoprotein lipase releases the free fatty acids and glycerol for their specific use.

Water-Soluble Vitamins
All vitamins and minerals are essential components of enzymes and co-enzymes.
Enzymes speed up the chemical reactions necessary for human bodily functions such as
energy production and metabolic processes, and they are the molecules that make
everything work. Many enzymes are in the mitochondria (cell energy production centre).

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Co-enzymes are molecules that help the enzymes in their chemical reactions. The main
components of enzymes are proteins, minerals and some vitamins; a lack of or deficiency
of their specific minerals and vitamins will prevent their function. Water-soluble vitamins
are all the B vitamins and vitamin C.

 Ascorbic acid (C) – synthesised by many animals such as primates, fruit bats,
guinea pigs and some birds. Because of a lack of the last enzyme (gulonolactone
oxidase) in the vitamin C pathway, humans are among the species that have lost
the ability to make it.

The main sources of vitamin C are vegetables and fruits. The highest are acerola,
red chilli, guavas, bell peppers, kale and parsley. Many others contain much less
vitamin C, including oranges, although they are most consumed. Vitamin C is a
very unstable molecule – heat, processing, exposure to light and alkali will all
destroy it. Even though vitamin C is easily absorbed, zinc and pectin (found in
apples) will reduce its absorption.

Vitamin C functions mainly as an antioxidant. It is a reduction agent; it donates a

hydrogen molecule to reverse oxidation. Vitamin C is a co-factor for a number of
hydroxylation reactions such as collagen, carnitine, neurotransmitters and tyrosine
synthesis as well as its catabolism. Vitamin C interacts with iron, lead, copper and
vitamin E.

Ascorbic acid deficiency will cause scurvy, some of the symptoms of which are
bleeding gums, petechiae (rupture of small blood vessels), poor wound healing,
excessive bruising and joint pain. Other symptoms of low vitamin C include
susceptibility to infections and depression and low iron uptake, especially in
vegan and vegetarians. People with alcohol abuse, diabetes and poor diet have a
higher need of the vitamin.

 Thiamin (B1) – main sources are meat (pork), legumes, whole or enriched grains,
yeast and wheat germ. Thiamin is destroyed by alkaline conditions and
temperatures above 100°C, and by the preservative sulphur dioxide. An enzyme
found in raw fish (thiaminase) and polyhydroxyphenols found in tea, coffee, nuts,

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blueberries, blackcurrants, red cabbage and Brussels sprouts can also inhibit its
absorption.

Thiamin functions as a co-factor for the thiamin pyrophosphate enzyme (TPP),

which is involved in the energy transformation, the synthesis of pentoses and
nicotinamide adenine dinucleotide phosphate (NADPH – more in later lessons),
and in the membrane and nerve conduction. Deficiency of B1 causes beriberi,
which ranges from symptoms like anorexia and muscle weakness to respiratory
problems. Alcoholism is one of the leading causes of thiamin deficiency as well as
for all the other B vitamins.

 Riboflavin (B2) – sources are milk and its products, yeast, eggs, meat, green leafy
vegetables, legumes, mushrooms, almonds, and minor amounts in fruits,
vegetables and cereal grains (if fortified).

Riboflavin functions as a co-enzyme in the form of flavin mononucleotide (FMN)

and flavin adenine dinucleotide (FAD) in a variety of oxidative enzyme systems in
energy production, and other pathways, including folate metabolism. Flavin is
mostly found in the liver, heart and kidney as well as a variety of tissues. The
conversion of flavin into FMN and FAD is under hormonal regulation
(antidiuretic hormone, aldosterone and thyroid hormones).

Deficiency of flavin causes cracked lips and corners of the mouth (angular
stomatitis), inflamed tongue, visual disturbance, and other disorders of the skin
and mucous membranes. B2 taken in supplement forms of over 1.7mg will make
the urine a fluorescent yellow-green, which is normal.

 Niacin (B3) – also termed nicotinic acid and nicotinamide, as well as niacinamide.
Nicotinic acid and nicotinamide are the active form of B3. Sources of B3 are tuna,
halibut, beef, chicken, turkey, pork and other meats, cereal grains, seeds, legumes,
as well as some made by the body from tryptophan (B6 and B2 are needed for the
conversion). In the animal form, niacin is found as nicotinamide adenine
dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP).

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Niacin is unavailable in certain foods such as corn or wheat and other cereal
grains, but corn treated with lime will make niacin available for absorption.
Niacin is stable in light, heat and air, but is lost in water when cooked. Niacin
absorption depends on its intestinal concentration – at low concentration, niacin is
absorbed via sodium-dependent, or carrier-mediated or facilitated diffusion; at
high concentration it goes through passive diffusion. NAD and NADP are the
hydrogen donors or electron acceptors for more than 200 enzymes. They are used
in the Kreb cycle, glycolosis, synthesis of fatty acids, cholesterol and steroids,
hormone synthesis, glutamate oxidation (glutamine), synthesis of DNA and
alcohol oxydation.

Deficiency of niacin will cause the condition called pellagra. This includes the four
‘D’ symptoms – dermatitis, dementia, diarrhoea and death. Deficiency might
occur in the case of alcoholism, malabsorption disorders, stress, trauma and
prolonged fever.

 Pantothenic acid (B5) – found in all plants, animal foods, such as meats (liver), egg
yolk, legumes, whole grain cereals, mushrooms, broccoli, avocados, yeast,
peanuts, soya beans etc. Pantothenic acid is found in food as part of coenzyme A
(CoA), which when digested is hydrolised into pantetheine and pantothenic acid.
Its main function is being part of CoA, which is used in the production of
energy-using fats and carbohydrates, in the synthesis of adrenal hormones and red
blood cells.

B5 is often considered the anti-stress vitamin for its role in the adrenal function.
CoA is also involved in the alternation of proteins, metabolism of certain drugs
and xenobiotics (chemicals not usually found in humans). Deficiency is rare and it
usually occurs in severe malnutrition, alcoholism, diabetes mellitus and
inflammatory bowel disorders. Symptoms of deficiency are the ‘burning feet
syndrome’ that many elderly people complain of. Taking calcium pantothenate
helps the syndrome.

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 Biotin – another vitamin that can be found widely in foods such as liver, soya
beans, egg yolk, cereals, legumes, nuts, brewer’s yeast and brown rice. Biotin is
also made by the intestinal bacteria, but it is not clear if it is absorbed from that. It
is absorbed by passive diffusion and actively with the need for sodium.

Biotin is a co-enzyme for many enzymes, including the Kreb cycle enzymes, fatty
acids synthesis, and the catabolism of the amino acid leucine. Activation of biotin
requires the presence of magnesium.

Deficiency symptoms are depression, hallucinations, muscle pain, anorexia, hair

loss (alopecia), nausea, scaly dermatitis and seborrhoea. In infants, cradle cap is
thought to be caused by a lack of intestinal bacteria, and adults who consume raw
egg whites in excess are at risk of biotin deficiency, as avidin in egg white will
prevent its absorption. (Often sports people eat raw egg white for its protein
content.) Intestinal bowel disorders, low HCL, alcoholism, anti-convulsive drugs
and sulphonamide therapy can all lead to biotin deficiency.

 Pyridoxine (B6) – can be found in three forms – pyridoxine phosphate (PNP),

pyridoxal phosphate (PLP) and pyridoxamine phosphate (PMP). All forms of B6
are found in bananas, haricot beans, walnuts, sirloin steak, salmon, chicken,
brewer’s yeast, sunflower seeds, wheat germ, lentils and other legumes. Heating,
canning and freezing can destroy the vitamin. In order to be absorbed vitamin B6
needs to be dephosphorylated (phosphate taken out).

B6 functions as co-enzyme for a variety of enzymes, mainly involved in amino

acid metabolism, such as decarboxylation of amino acids (production of histamine
from histidine and dopamine from serotonin), transamination, which is the
synthesis of essential amino acids from non-essential amino acids, such as
nicotinic acid from tryptophan and cysteine from methonine (mainly PLP and
PMP). B6 is also involved in fat and glycogen, especially in muscles, and haem
synthesis.

Deficiency of B6 is rare and occurs mainly in elderly people eating a poor diet,
infants with low plasma B6 vitamin, alcoholism, kidney problems, people taking

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corticosteroids, anti-convulsant drugs and penicillamine. Symptoms of deficiency

include depression, convulsions, glucose intolerance, cheilosis, glossitis, stomatitis,
neurological problems and anaemia due to impaired haem synthesis.

 Folic acid – the generic term is folate or folacin. Sources of folic acid are
mushrooms, green vegetables, such as spinach, Brussel sprouts, broccoli, Swiss
chard, cabbage, asparagus, turnip greens, brewer’s yeast, legumes and liver. Raw
vegetables are the best sources, as cooking will destroy the vitamin, as well as heat
and light.

Folate is found in food as polyglutamate and in order to be absorbed it needs to be

hydrolised to monoglutamate form. The enzyme for this action needs zinc to
function, and it is inhibited by alcohol. Folate is involved in amino acid
metabolism such as the synthesis of serine from glycine, conversion of histidine to
glutamic acid, synthesis of purine and pyrimidine for DNA and RNA and
methionine synthesis.

High levels of homocysteine, due to a deficiency of B12 and folate, have been
connected to heart diseases (methionine synthesis). Deficiency causes
megaloblastic anaemia (release of large immature erythrocytes, failure of cell
division). Other symptoms related to folate deficiency are depression, dementia
and cancer. Alcohol, low HCL, irritable bowel disease, oral contraceptives,
pregnant and lactating women will be at risk of folate deficiency. Vitamin C
prevents the oxidation of folate, while zinc absorption will be reduced with high
folate intake.

 Cobalamin (B12) – found mainly in animal sources, such as meat and meat
products, poultry, fish and shellfish, eggs and dairy products. For vegans,
brewer’s yeast and fermented food such as tempeh can be a minor source, but
there are doubts on the bioavailability of B12 from these sources. This is one of the
reasons that people who follow a vegan diet from an early age are in danger of B12
deficiency in adult life, if not earlier. Cobalamins have one molecule of cobalt and
when ingested they need to be released from their polypeptides from the enzyme

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 Nutrition Course – The Scientific Approach: Lesson Three

pepsin in the stomach. High dosage of vitamin C (more than 500 mg) and folate
(more than 5 mg), reduce the bioavailability of B12 if ingested at the same time.

In order to be absorbed, B12 needs two proteins that are found in the stomach –
one is the intrinsic factor (IF) and the other is the ‘R’ proteins (cobalophilins or
haptocorrins). The ‘R’ proteins have a high affinity for the cobalamins, and once
they are released in the stomach, they attach to each other and get transported to
the small intestine, where the complex is hydrolysed by the pancreatic proteases
and B12 is freed again. The IF binds in the small intestine to the free cobalamins
forming the cobalamin-IF complex. Here the complex attaches to the receptors in
the ileum and gets absorbed into the blood stream.

B12 is a co-factor for the enzyme methyl-transferase, which transfers a methyl

group from one molecule to another. It is used in the enzymatic reactions as
methylcobalamin in the conversion of homocysteine into methionine by releasing
the tetrahydrofolate (THF) from the methyl complex N5 methyl-tetrahydrofolate.
This pathway is important for the formation of methionine, therefore reduction of
homocysteine, DNA synthesis and cells division. B12 is also used as a co-factor for
fatty acid synthesis, in the form of adenosylcobalamin (CoA mutase), and L-
leucine catabolism.

Deficiency of B12 will prevent cell division and therefore lead to megaloblastic
anaemia (bigger cell), as well as neurological damage (myelin sheath damage) that
can be undetected if high folate is supplemented (above 5 mg). B12 deficiency can
occur after many years on a vegan diet, alcohol abuse, with potassium
supplements and long standing low HCL.

© Copyright Reserved

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 Nutrition Course – The Scientific Approach: Lesson Three

BIBLIOGRAPHY

Barasi M. E. (2003). Human Nutrition. 2nd ed. New York: Oxford University Press.
Celiberto L. S. et al. (2015). Probiotis: The scientific evidence in the context of
Inflammatory Bowel Disease. Critical Reviews in Food, Science and Nutrition; May 21:0.
Damasco D., Kolios G. (2008). Probiotics and Prebiotics in Inflammatory Bowel Disease:
microflora ‘on the scope’. British Journal of Clinical Pharmacology. 65 (4) April.
Groff J. L., Gropper S. S. (2000). Advanced Nutrition and Human Metabolism. 3rd ed.
London: Thomson Learning; also 6th ed. (2012) same book. Gropper S. S., Smith J.,
Wadsforth; CA.
Heba S. et al. (2014). Dysbiosis of salivary microbiota in Inflammatory Bowel Disease and
its association with oral immunological biomarkers. DNA Research 21.
Kunai T. et al. (2015). A breakthrough in probiotics: Clostridium butyricum regulates gut
homeostasis and anti-inflammatory response in inflammatory bowel disease. Journal of
Gastroenterology, May 5.
Matsuoka K., Kanai T. (2015). The gut microbiota and inflammatory bowel disease.
Seminars in Immunopathology. January 37 (1).
Meijer B. J., Dieleman L. A. (2011). Probiotics in the treatment of human Inflammatory
Bowel Diseases: update 2011. Journal of Clinical Gastroenterology. November; 45 Suppl.
Millan J. et al. (2009). Lipoproteins ratio: Physiological significance and clinical
usefulness in cardiovascular prevention. Vascular Health and Risk Management.
5 September.
Murray M., Pizzorno J., Pizzorno L. (2005). The Encyclopaedia of Healing Foods. New
York: Atria Books.
Sartor R. B. (2004). Therapeutic manipulation of the enteric microflora in Inflammatory
Bowel Diseases: antibiotics, probiotics and prebiotics. Gastroenerology. 126 (6) May.
Tang J. E. et al. (2009). Ingestion of whey hydrolysate, caseinx, or soy protein isolate:
effects on mixed muscle protein synthesis at rest and following resistance exercise in
young men. Journal of Applied Physiology. 107 (3) September.
Tortora G. J., Derrickson B. H. (2009). Principles of Anatomy and Physiology.
12th ed., vol. 1 & 2. Asia: John Wiley & Sons.
Veerappan G. R. et al. (2012). Probiotics for the treatment of Inflammatory Bowel
Disease. Current Gastroenterology Reports; August; 14 (4).

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Wang Z. K. et al. (2014). Intestinal microbiota pathogenesis and fecal microbiota

transplantation for Inflammatory Bowel Disease. World Journal of Gastroenterology
October 28; 20 (40).

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Nutrition Course – The Scientific Approach: Lesson Three
Notes
Nutrition Course – The Scientific Approach: Lesson Three
Notes
 THE BSY GROUP

NUTRITION COURSE – THE SCIENTIFIC APPROACH

QUESTIONS ON LESSON TWO

1) What constitutes the endocrine system and what are the major glands and organs
involved in its function?
2) What are amines? Give three examples.
3) How does negative feedback control work? Give one example of negative
feedback.
4) Which of the major glands is responsible for maintaining the body’s homeostasis?
Explain how it does this.
5) What are the two main thyroid disorders?
6) What are the symptoms of the two main thyroid disorders? List at least six
symptoms for each disorder.
7) Which foods can be especially beneficial for the thyroid gland?
8) What are natural goitrogens? List some of the foods that contain these.
9) Which minerals are essential for normal thyroid metabolism?
10) Write how parathyroid hormone (PTH) production can increase or decrease
according to mineral intake.

Answer the questions as fully as possible, leaving at least two lines clear after each answer
for the tutor’s comments. Please do not use pencil or red ink. Both hand written and type
written answers are acceptable.

Complete this paper with your name and address below, and return it together with your
answer papers to The BSY Group.

STUDENT NUMBER ...........................................

NAME (MR/MRS/MISS/MS/DR) ........................................................................

ADDRESS ...................................................................................................................

.......................................................................................................................................

.......................................................................................POSTCODE .........................