21/07/2015

151.232 NUTRITION AND

METABOLISM
Protein (part 1)
Dr Cath Conlon
c.conlon@massey.ac.nz
IFNHH, 2015

Learning objectives

Learning objectives

Describe the chemical structure of proteins.

Discuss the processes of protein digestion and

absorption. Describe protein synthesis.

Describe the structure of amino acids, and explain

how their sequence in proteins affects the proteins'
shapes.

Briefly discuss the function and roles proteins play

in the human body.

Define what an essential, non-essential and

conditionally essential amino acid is.

Discuss protein requirements and how

requirements are estimated.

A chemists perspective

What are Proteins?

Essential organic compounds made of smaller building
blocks called amino acids
Form vital structural and working substances in all cells of
the body
70kg man contains about 11kg (16%) of proteins
(nearly found as skeletal muscle)
Unlike fats and carbohydrate, the body does not
maintain an energy storage form
Found in a range of animal and plant foods

Proteins contain the same atoms as CHO & lipids

Carbon (C)
Oxygen (O)
But also contain nitrogen (N)
These nitrogen atoms give the name amino (nitrogen
containing) to amino acids the links in the chain of
proteins

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Amino Acids

Amino Acids
20 different aa
Sequence of aa in each protein which determines its
unique shape & function
Side groups (r group) vary from one aa to the next
making proteins more complex than CHO or lipids
aa share common structure but differ in size, shape,
electrical charge and other characteristics due to diff in
side groups

Examples:

Glycine

Simplest aa
with hydrogen
side group

Amino Acids

Not Essential

Alanine

Aspartic acid

More complex side groups

Phenylalanine

Essential amino acids (also called indispensable amino

acids)
9 aas that the body cannot make at all or in
sufficient quantities
Must be obtained from food
Non-essential amino acids (also called dispensable
amino acids)
The body can synthesise itself
Conditionally essential amino acids
Become essential under certain physiologic conditions

You need to be able to give examples

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More than half of the aa are non essential meaning the

body can synthesise them for itself. Proteins in foods often
deliver these non essential aa but its not essential that they
do.
The body is able to make all the non-essential aa given
nitrogen form the amino group and fragments from CHO
and lipids to form the rest of the structure
9 essential aa that must be supplied by the diet

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Phenylketonuria
Example of a conditionally essential aa is tyrosine
- essential in PKU
Autosomal
recessive disorder
inherited error of
metabolism
Phenylalaine
normally converted
to Tyrosine which
enters Krebs cycle
PKU results in
elevated blood
levels of
phenylalaine
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PKU; treatment and prevention

Tyrosine must be supplied by diet
Phenylalanine intake must be carefully restricted; THIS
AMINO ACID IS STILL IMPORTANT FOR GROWTH,
ETC.
All infants are tested for PKU at birth

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Proteins

Transamination
Transfer of the amine group from an essential amino acid
to a different acid group and R group
The acid groups and R groups can donated by amino acids
or they can be made from the breakdown products of CHO
and lipids
This is also the process by which we make non essential
aa

Cells link aa end to end in a variety of sequences to

form 1000s of diff proteins
Linked by peptide bonds

Condensation
reaction

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Proteins
Polypeptide eg insulin small protein 51 aa which
consists of 2 polypeptide chains linked by disulphide
bridges which always involve aa cysteine (r group
contains sulphur)

Primary structure of a protein

It is the sequence of amino acids that makes each
protein different from the next
Huge variety of polypeptide chains (more complex than
CHO or lipids)

Dipeptide = 2 amino acids

Tripeptide = 3 amino acids
Polypeptide = many amino acids
Most proteins have many 100 amino
acids
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4 levels
Primary: sequence of AAs
Protein
which are linked together
Secondary: conformations
of the polypeptide
backbone
Tertiary: folding secondary
structures into a compact
globular protein
Quaternary: arrangement
of subunits into a single
functional protein

Protein
shape
and
function

structure

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Protein Function is Altered by

Denaturation

ApoE protein is involved in the transportation of cholesterol and

other lipids.
There are 3 isoforms which are genetically determined depending
on whether you have arginine or cysteine at positions 112 and
158.
These single AA differences alter the proteins structure and
conformation and influence how cholesterol is dealt with.
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People carry ApoE4 are at higher risk of CVD(Bu, 2009)

What Happens
to the Protein You Eat?

Uncoiling of protein that changes its ability

to function
If proteins are subject to heat, acid or other
conditions that affect their stability they
become denatured
Examples
Food: hardening of an egg when it is
cooked, curdling of milk when acid is
added.
In stomach: acid denatures proteins
aids digestion and kills pathogens
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Protein digestion
Proteins in foods do not become body proteins!
They supply aa from which the body makes its own
proteins
Food containing protein
Long polypeptide strands
Shorter strands
Shorter strands
Tripeptides
Dipeptides
Amino acids

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Simplified version of digesting protein

Protein
Digestion in
the GI Tract

Protein digestion and absorption in the small

intestine
1. brush-border membrane
peptidases
2. brush-border membrane
amino acid transporters
3. brush-border membrane
di- and tripeptide
transporters
4. intracellular peptidases
5.basolateral-membrane
amino acid carriers
6. basolateral membrane diand tripeptide carriers

Protein absorption
Intracellular peptidases digest absorbed di- and
tripeptides. (90% or more appear in the portal blood as
free amino acids).
Absorption of amino acids and peptides is
developmentally regulated and is influenced by diet,
hormones and growth factors.
A high protein diet - upregulation of peptide and most
amino acid transport. Short term fasting increases
absorption rates, but long term fasting decreases amino
acid transport with little change in peptide absorption.
Absorbed amino acids (especially glutamine, glutamate,
and aspartate) are the major respiratory fuels for the
small intestine. 10% of the absorbed amino acids are
used for protein synthesis within the enterocyte.

Protein myths

Protein synthesis

You can ingest enzymes and they will work

Consuming amino acid supplements will be beneficial
saves the body having to break down proteins
Whole proteins better as the body dismantles and
absorbs aa at optimal rates

In adults 4g/kg body weight of protein is

synthesised each day
In infants 12g/kg of body weight falls to 6g/kg
by 1 year
In adults in steady state protein synthesis is
matched by an equivalent rate of protein
degradation protein balance
In infancy, childhood & pregnancy protein
synthesis exceeds protein degradation (positive
protein balance). Accounts for the deposition of
tissues accompanying growth
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Protein Synthesis

Protein Synthesis

Protein Synthesis

Body contains about 30,000 different kinds of proteins.

Each human being is unique because of the small
differences in the bodys proteins.
These differences are determined by the amino acid
sequence of proteins which in turn are determined by
genes.
Process we have just described - how cells synthesize
proteins according to the genetic information provided
by the DNA in the nucleus of each cell.
This information dictates the order in which amino
acids must be linked together to form a given protein.
Sequencing errors occasionally occur sometimes with
significant consequences eg sicke cell anaemia.

Sequencing errors
Functions of proteins
Functional diversity
Cell membrane structure & function
Enzymes
Hormones & other chemical messengers
Immune functions
Fluid balance
Acid-base balance
Transport
Source of energy & glucose

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Structural & maintenance

Enzymes

Provide building materials for growth and maintenance

Collagen
Bone & Skin
Keratin
Hair & nails
Motor proteins
Muscles

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Immune function

Hormones
Chemical messengers that are made in one part
of the body but act on cells in another part

Lymphocytes produce antibody proteins that fight

antigens that invade the body
Provide immunity

Fluid balance

Proteins help maintain volume & composition of body fluid

Acid-Base balance

Act as buffers to help maintain acid-base balance of body fluids

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Transport Proteins

Fluid Balance
Plasma proteins attract water - oedema can result when get
plasma proteins entering interstitial spaces faster than can
be cleared by lymphatic system.
Protein related causes include excessive protein losses eg
kidney disease or large wounds, inadequate synthesis or
inadequate intake or inadequate levels plasma proteins.

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Blood clotting
There are 13 blood clotting proteins (coagulation factor)
found in the blood. If one factor is missing or present at low
levels, this causes hemophilia and other blood clotting
problems and a proper clot will not form.

Source of energy & glucose

Proteins provide some fuel for the bodys energy needs
Body will use protein if insufficient energy or glucose
provided by the diet

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Protein metabolism protein turnover and aa

pool

Body composition

Homeostasis:Hormones
Acid-base balance
Immunity

Formation of enzymes

Uses of protein

Blood clotting

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Proteins continually being made and broken down

protein turnover
When protein break down free aa which mix with aa
from dietary protein forms the aa pool within cells and
circulating blood
Rate of protein degradation and protein intake may vary
BUT pattern of aa within the pool is constant
Regardless of source pool of aa used to make body
proteins or other N containing compounds or stripped of
N & used for energy (or stored as fat)

Other functions:
Energy
Hair, nails, bones
Synthesis

Transport

Summary of uses of protein

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Nitrogen balance

Nitrogen balance

Because all protein contains 16% nitrogen by weight a

simple chemical analysis of nitrogen can be used as a
means of calculating how much protein the nitrogen has
come from
To convert nitrogen values to protein values multiply by 6.25
(100/16)

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Nitrogen balance is a measure of the relationship between

the amount of nitrogen taken into the body and the amount
excreted in urine, faeces and skin
+ve bal Nitrogen intake > nitrogen loss
-ve bal Nitrogen loss > nitrogen intake
Equilibrium Nitrogen intake = nitrogen loss

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Nutritional importance of proteins

Nutritional values determined by its primary structure (ie
amino acid composition)
Tertiary structure can influence protein digestibility
Globular proteins are generally more easily digested than
filamentous proteins such as collagen, elastin and keratin

151.232 NUTRITION AND

METABOLISM
Protein (part 2)
Dr Cath Conlon
c.conlon@massey.ac.nz
2015

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Protein quality and amino acid profile

Learning objectives
List factors that affect the quality of dietary protein.
Define a complete protein.
Describe the health consequences of ingesting
inadequate or excess protein.
Describe marasmus and kwashiorkor. Discuss how
the two conditions can be distinguished, and the
ways they overlap.
List the factors that are considered in establishing
recommended protein intakes.

Protein quality
Kind of amino acids contains
Proportion in which they are present
Amino acid profile relative proportions in which essential
amino acids are present in the protein

Are we generally worried about protein intakes in

NZ?

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Types of protein

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Limiting amino acid

Complete or high biological value (high quality)

Contain all essential amino acids in proportions capable
of promoting growth
Incomplete or low biological value (low quality)
Proteins that lack or have limited amounts of one or
more essential amino acids, incapable of promoting
growth (if sole proteins in diet)

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Some proteins that contain all the essential aas but

relatively small amounts of one aa. These proteins have
sufficient aa to promote repair of body tissues but not
enough to promote growth
aa that present in smallest amount required for growth is
called limiting amino acid
Legumes methionine
Cereal protein - lysine

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Complementary proteins

Animal vs Plant
Animal derived protein from meat, fish, poultry, eggs and
dairy
Generally provide high-quality protein
Have high digestibility (90-99%)
Plant derived protein from vegetables, nuts, seeds,
gains and legumes
Often tend to be limiting in 1 or more essential aa
Generally less digestible

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Evaluation of proteins

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Requirements for protein

Several biological measures and chemical measures are

used to evaluate protein quality.
Biological Value (BV)
Net Protein Utilisation (NPU)
Protein Efficiency Ratio (PER)
Chemical (amino acid) Score

Varies with age & physiological state

Based on quantity of aa required to support optimum
health
Definition: requirement is the intake needed to prevent
loss of body protein and to allow for adequate deposition
or production of protein during growth, pregnancy or
lactation FAO/WHO/UNU

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Requirements for protein

What is the composition of protein that

we need?

As close as possible to aa ratios found in human proteins

Good sources of complete proteins animal sources

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AMDR

How much protein do we eat in NZ?

= acceptable macronutrient ranges for

macronutrients to reduce chronic disease
Protein = 15% to 25% energy
Many diets for weight loss recommend
up to 30%

Usual daily median

intake (g)
1997
2008/9

RDI (g/day)

Males

105

102

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Females

71

71

46

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PROTEIN SOURCES IN NZ DIET . NNS

NNS 2008/9

1997 Age 15+

beef and veal

milk
bread
poultry
fish/seafood
bread based dishes
pork
potatoes and kumara
sausages
cheese
vegetables
grains and pasta

14% [f = 12% m = 15%]

10% [f = 11% m = 9%]
11% [f = 11% m = 10%]
7% [f = 8% m = 7%]
7% [f = 7% m = 7%]
5% [f = 4% m = 6%]
5% [f = 5% m = 5%]
4% [f = 4% m = 4%]
4% [f = 3% m = 4%]
4%
4%
3%

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PROTEIN SOURCES IN NZ DIET .

PROTEIN SOURCES IN NZ DIET .

NNS 2008/9 Age 15+

CNS02* Age 5-14

bread
poultry
milk
beef and veal
grains and pasta
bread based dishes
fish/seafood
pork
vegetables
potatoes and kumara
sausages
cheese

11.1% [f = 10.7% m = 11.4%]

8.8% [f = 8.8% m = 8.8%]
8.8% [f = 9.4% m = 8.1%]
7.8% [f = 7.3% m = 8.2%]
6.8% [f = 6.6% m = 7.1%]
6.6% [f = 5.4% m = 7.8%]
6.0% [f = 6.3 % m = 5.6%]
4.5% [f = 3.9% m = 5.2%]
4.3% [f = 5.0% m = 3.5%]
3.2%
3.1%
3.1 %

beef and veal

milk
bread
poultry
fish/seafood
bread based dishes
potatoes and kumara
Sausages/processed
meats
grains and pasta

8% [f = 8% m = 9%]
11% [f = 11% m = 11%]
13% [f = 14% m = 13%]
9% [f = 9% m = 9%]
4% [f = 3% m = 5%]
5% [f = 4% m = 6%]
4% [f = 4% m = 4%]
4% [f = 4% m = 5%]
5%

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CNS02 results - Protein

Practical advice
Protein in the diet is provided by a wide range of
available foods, including lean meat, chicken,
seafood, eggs & milk. Bread is also an important
source
Choose low & reduced fat options from the meat
and milk food groups where possible
If vegetarian, include protein from diverse plant
sources (legumes, nuts, breads & cereals). If lactoovo vegetarian, also include eggs and milk
products

Median usual daily intake in NZ children ranges: Males 5-6 years 52g; 11-14 years 88g
Females 5-6 years 52g; 11-14 years 66g

NZ children consuming at least double their age

specific RDIs

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Protein energy malnutrition (PEM)

Protein deficiency and excess

Deficiency syndrome caused by inadequate intake of

macronutrients
Characterised by an energy deficit in all macronutrients &
many micronutrients
Common in developing countries but can occur in
persons of any age in any country

Can you eat too much protein?

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Poverty and hunger, children aged < 5yrs underweight (%)

WHO statistics, latest available figures since 2000

PEM
Most lethal form of malnutrition by far
Assoc with >50% of the 10.9 million child deaths each year
Globally children who are poorly nourished suffer up to 160
days of illness each year
Malnutrition magnifies the effects of every disease
WHO

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Hunger
In many African languages there are two types of
words for hunger.
The first is hunger that goes away (mild), even
when it is visible. The other is hunger that you
cannot survive (severe).
Examples of hunger words that have become
part of the international lexicon are:
Kwashiorkor--"the disease that the first child gets
when the new child comes"
Marasmus--"to waste away"

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Marasmus

PEM classification & Etiology

There are 3 forms of acute malnutrition:
Marasmus severe weight loss or wasting (dry
form)
Kwashiorkor bloated appearance due to water
retention (bi-lateral oedema wet form)
Marasmic-kwashiorkor a combination of both
wasting and bi-lateral oedema.
Forms depends on balance of non-protein and protein
sources of energy

Marasmus is the most common form of acute

malnutrition in nutritional emergencies and, in its
severe form, can very quickly lead to death if
untreated
Characterised by severe wasting of fat and
muscle which the body breaks down to make
energy.
Skin and bones appearance
A thin old man face

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Marasmus

Dry (thin, desiccated), form of Protein-Energy

Malnutrition
Results from near starvation with deficiency of protein
and non protein nutrients.
The marasmic child consumes very little food often
because mother is unable to breastfeed
Child is very thin from loss of muscle and body fat.

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Marasmus
Energy intake is insufficient for the body's
requirements, body draws on its own stores.
Liver glycogen is exhausted within a few hours
skeletal muscle protein is then used via
gluconeogenesis to maintain adequate plasma
glucose.
Triglycerides (fat depots) are broken down into
FFAs, to provide some energy for most tissues not nervous system.
When near starvation is prolonged, fatty acids are
incompletely oxidized to ketone bodies, which can
be used by the brain
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Kwashiorkor condition resulting from

inadequate protein intake

Kwashiorkor
African word meaning "first child-second child. First child
develops PEM when the Second child replaces first child
at the breast

Early symptoms include fatigue,

irritability, and lethargy.
As protein deprivation continues,
growth failure, loss of muscle mass,
generalised swelling (oedema) and
decreased immunity.
Large, protuberant belly is common.
The incidence of kwashiorkor in
industrialized countries is extremely
small.
Typically found in countries where
there is drought and famine.

Wet (oedematous, swollen) form of

Protein-energy Malnutrition
Characterised by bilateral pitting
oedema
Protein deficiency usually
more marked than the
energy deficiency
Children with kwashiorkor tend to be
older than those with marasmus develop disease after weaning.
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Marasmic-Kwashiorkor mix
Combination of the oedema of kwahiorkor and the
wasting of maramus
It may be 2 stages of the same condition
Some research indicates that marasmus
represents the bodies adaptation to starvation,
while kwashiokor develops when adaptation fails

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Excess protein
Overconsumption offers no benefits and may
contribute to some conditions (?)
Obesity
CVD
Some cancers (e.g. colon, breast, prostrate)
But animal protein also often high in saturated fat
effects of each difficult to separate
May also displace fruits, vegetables and grains in
diet ( micronutrient defic.)

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