BIOKIMIA PANGAN

TPP 2313

PS ILMU & TEKNOLOGI PANGAN (ITP) UNSOED

 Living organisms are made up of organic
molecules and use organic molecules to
function.

There are four basic groups of organic

compounds in the body: Carbohydrates, Lipids
(fats), Proteins and Nucleic acids.
Biochemistry – study of the chemistry of living organisms

• All organic compounds will have the element carbon in them

Exception: CO2 is not organic (CO2 is not
composed of living substances.)
• Organic compounds are usually complex compounds with
many atoms in their structure.
Ex: Glucose – C6H12O6

• Four kinds of organic compounds:

1. Carbohydrates
2. Lipids
3. Proteins
4. Nucleic acids – DNA and RNA
 Organic Substances of the Body
Organic Elements Building Blocks
Compound

Carbohydrates Carbon, Hydrogen Simple sugars

and Oxygen (monosaccharides)

Lipids Carbon, Hydrogen Glycerol and Fatty

and Oxygen Acids

Proteins Carbon, Hydrogen, Amino Acids

Oxygen, Nitrogen,
Phosphorus and
Sulfur
Nucleic Acids Carbon, Hydrogen, Nucleotides
(DNA and RNA) Oxygen, Nitrogen
and Phosphorus
 • control rate of
reactions
Proteins • form bones and
Function muscles
• transport substances in
and out of cells
• fights disease
Structural
Formula of Amino • food examples from
Acid: animals – eggs, milk,
Examples meat
(not in the • food examples from
reading)
plants – nuts, beans
• enzymes

• elements involved –
C, N, H, O
• proteins are composed
of – amino acids
Structure
• How many different
amino acids are there?
20
 • store and
transmit genetic
Function information
(parent to
offspring)
Nucleic
Acids

• DNA
Examples
• RNA
Introduction to Food Proteins and Enzymes

 Proteins play a central role in biological systems.

 Enzymes perform the biochemical processes that
sustain the life of a cell/organism.
 Proteins (such as collagen and keratin) also function as
structural components of cells and complex organisms.
 The functional diversity of proteins arises from their
chemical makeup. Proteins are highly complex
polymers, made up of 20 different amino acids.
 Protein synthesis occurs in ribosomes. After the synthesis, some
amino acids are modified by cytoplasmic enzymes which changes
the composition of some proteins.

 Proteins that are not enzymatically modified in cells are called

homoproteins, and those that are modified or complexed with
nonprotein components are called conjugated proteins or
heteroproteins.

 The nonprotein components are referred to as prosthetic groups.

-Examples of conjugated proteins include nucleoproteins
(ribosomes), glycoproteins (casein), phosphoproteins (kinases,
phosphorylases), lipoproteins (proteins of egg yolk, plasma
proteins), and metalloproteins (hemoglobin, and several enzymes).
Structure of protein

.
 Globular proteins
are exist in spherical shapes, resulting from folding of the polypeptide
chain(s) on itself.

 Fibrous proteins
are exist in rod-shapes containing twisted linear polypeptide chains (e.g.,
collagen, keratin, and elastin). Fibrous proteins also can be formed as a result
of linear aggregation of small globular proteins, such as actin and fibrin.

 A majority of enzymes are globular proteins, and

 fibrous proteins function as structural proteins.
Biological functions of proteins :
 Enzyme catalysts,
 Structural proteins,
 Hormones (insulin and growth hormone),
 Transfer proteins (serum albumin and hemoglobin),
 Antibodies (immuno-globulins),
 Storage proteins (egg albumen and seed proteins),
Storage proteins are found in eggs and seeds. These proteins act as
sources of nitrogen and amino acids for germinating seeds and embryos
 Protective proteins (toxins and allergens).
Protective proteins are a part of the defense mechanism for the survival
of certain microorganisms and animals.
 All biologically produced proteins can be used as food proteins.
However, for practical purposes, food proteins may be defined
as those that are easily digestible, nontoxic, nutritionally
adequate, functionally useable in food products, and available
in abundance.

 Traditionally, milk, meats (including fish and poultry), eggs,

cereals, and oilseeds have been the major sources of food
proteins. However, because of the increase in world
population, nontraditional sources of proteins for human
nutrition need to be developed to meet the future demand.

 The suitability of such new protein sources for use in foods,

however, depends on their cost and their ability to fulfill the
normal role of protein ingredients in processed and home-
cooked foods.
Functions of Food Proteins
 Amino acids, peptides and proteins are important constituents of food.
-They supply the required building blocks for protein biosynthesis. -They
contribute to the flavor of food and are precursors for aroma compounds
.
 They contribute, with other food compounds such as carbohydrates, to
colors formed during thermal or enzymatic reactions in production,
processing and storage of food.

 Proteins contribute to food physical properties through their ability to

build or stabilize gels, foams, emulsions and fibrillar structures. -The
nutritional energy value of proteins (17 kJ/g or 4 kcal/g) is as high as that
of carbohydrates.
Sources of Food Proteins
 The most important sources of protein are grain, oilseeds and legumes, followed by meat
and milk.

 In addition to plants and animals, protein producers include algae (Chlorella, Spirulina
spp.), yeasts and bacteria (single-cell proteins [SCP])
.
 Bacteria of the species Pseudomonas in aqueous methanol produce about 0.3 ton of protein
per ton of alcohol.

 Some products rich in protein also result from other processes, e. g., in oil and starch
production.

 Protein concentrates and protein isolates serve to enhance the nutritional value and to
enhance of the physical properties of foods. They are added to traditional foods, such as
meat and cereal products, but they are also used in the production of novel food items
such as meat and milk substitutes.
Raw materials in which protein enrichment takes place include:
 Legumes such as soybeans,
 Wheat, which provide gluten as a by-product of starch production,
 Potatoes; after starch production, protein isolated by thermal coagulation,
 Eggs, which are processed into different products (e.g., whole egg, egg white and
egg yolk products),
 Milk, which supplies casein and whey protein,
 Fish, which supplies protein concentrates after fat extraction,
 Blood from slaughter animals, which is processed into blood meal, blood plasma
concentrate and globin isolate,
 Green plants grown for animal fodder, such as alfalfa, which are processed into leaf
protein concentrates through the thermal coagulation of proteins.
*Proteins are polymer of amino acids

*Amino acids are building block of protein

The R group determines the amino acid
Classification of Amino Acids

 Side chain (R group) classification.

 Biological classification.
 Metabolic classification.
1-Side Chain (R group)
Classification
 CHEMICAL CLASSIFICATION -The amino acids are
classified according to the chemical structure of the
side chain (R) into:
 Aliphatic
 Hydroxy
 Sulfur containing
 Aromatic
 Acidic
 Basic
 Imino acids
Side Chain Classification
Glycine
Non Polar (hydrophobic) Amino Acids

 Side chains of non polar (hydrophobic) amino acids can

not participate in hydrogen or ionic bonds, but they
form hydrophobic interactions.
 In aqueous environment, non polar amino acids tend to
be present in the interior of proteins.
 Non polar (hydrophobic) amino acids include: -Amino
acids with aliphatic R group (glycine, alanine). -Amino
acids with aliphatic branched R group (valine, leucine
and isoleucine). -Amino acids with aromatic R group
(phenylalanine, tryptophan). -Amino acids with sulfur
containing R group (methionine). -Imino acid (proline).
Amino acids with non polar side chains (Aliphatic)

Glycine(Gly - G)

Alanine (Ala – A)
Amino acids with non polar side chains (branched
chains,aliphatic)

Valine (Val – V)

Leucine (Leu – L)

Isoleucine (Ile
– I)
Amino acids with non polar side chains (Aromatic)

Phenylalanine (Phe – F)

Tryptophan (Trp – W)
Amino acids with non polar side chains (imino)

Proline (Pro – P)
Amino acids with non polar side chains
(sulfur containing)

Methionine (Met – M)
Polar (hydrophilic) Amino Acids

Side
chains of polar (hydrophilic) amino acids can participate in
hydrogen or ionic bonds.

Therefore, in aqueous environment polar amino acids tend to be

present on the surface of proteins.
Polar (hydrophilic) amino acids are classified into:
1. Polar charged amino acids:
 Acidic amino acids (aspartic & glutamic acids) and
Basic amino acids (arginine, lysine, histidine)
2.Polar uncharged amino acids:

 Amino acids with OH group (serine, threonine, tyrosine)

Amino acids with SH group (cysteine)
 Amino acids with amide group (glutamine, asparagine)
Amino acids with polar charged side
chains (acidic group)

Aspartic acid (Asp – D)

Glutamic acid (Glu – E)

Amino acids with polar charged side chains (basic group)

Lysine (Lys – K)

Arginine (Arg – R)

Histidine (His – H)
Amino acids with polar uncharged side
chains (with OH group)

Serine (Ser – S)

Tyrosine (Tyr – Y)

Threonine (Thr – T)
Amino acids with polar uncharged side
chains (with SH group)

Cysteine (Cys – C)
Amino acids with polar uncharged side chains (with
amide group)

Asparagine (Asn – N)

Glutamine (Gln – Q)
2-Biological (Nutritional) classification

On nutritional basis AA are classified into essential or non-essential AA.

1- Non essential amino acids:
Amino acids that could be synthesized in the body, so they are not
needed in the diet. They are 10 AA.

2- Essential amino acids:

 Amino acids that could not be synthesized in the body, so they have to
be taken in the diet, and their deficiency results in diseases.
 The essential amino acids are not more important to our body than
the non-essential amino acids.
 Both (all 20 AA) are equally needed and equally essential for the
normal growth and good health.
Biological classification
3-Metabolic classification
(According to their metabolic fate in the body )

 Glucogenic amino acids:

Amino acids that can give glucose.

 Ketogenic amino acids:

Amino acids that can give ketone bodies.

 Glucogenic/Ketogenic (mixed) amino acids:

Amino acids that can give both ketone bodies and glucose.
protein

 A major component of foods.

 It is digested firstly in the stomach, and then in

the duodenum to dipeptides and amino acid.

 Absorbed using symport active transport with

sodium.

 Stored in liver and muscles

Stages of Metabolism
• Energy-containing nutrients are processed in three
major stages:
 1. Digestion – breakdown of food; nutrients are
transported to tissues

 2. Anabolism and formation of catabolic

intermediates where nutrients are:
• Built into lipids, proteins, and glycogen or
• Broken down by catabolic pathways to pyruvic acid and acetyl
CoA.

 3. Oxidative breakdown – nutrients are catabolized to

carbon dioxide, water, and ATP
 Substrates Products
Catabolism

ADP + Pi ATP

PPi + AMP

Anabolism
Tissue
Components Precursors
ANABOLIC CATABOLIC
large complex organic Decomposition of large
molecules are constructed complex molecules into
from small molecules small molecules

Biosynthetic Degradative
c
Reductive Oxidative

Energy Required Energy Liberated

A simplified outline of the catabolism of
proteins, carbohydrates and fats
► Definition of nitrogen pool:

It include the free a.as distributed throughout the body

- The a.a. pool contains 100 gm a.as.50% of these a.as are in the form of
glutamate & glutamine (Why?)

- In contrast to the amount of protein in the body (about 12 Kg in 70 Kg man),

the a.a. pool is small (only 100 gm)

►Sources & fate of the a.a. pool:

Excess amino acids cannot be stored.
Surplus amino acids are used for fuel.
Carbon skeleton is converted to

Acetyl–CoA
Acetoacetyl–CoA
Pyruvate
Citric acid cycle intermediate
The amino group nitrogen is converted to urea and
excreted.
Glucose, fatty acids and ketone bodies can be formed
from amino acids.
 PROTEIN

Metabolisme protein
Protein digestion
Protein digestion
Protein Metabolism
 Non-essential amino acids can be formed by
transamination, transfer of an amine group
to keto acid.
 If used for energy, amino acids undergo
oxidative deamination. Ammonia and keto
acids are produced as by-products of
oxidative deamination. Ammonia is
converted to urea and excreted.
 Amino acids are not stored in the body
 Di decarboxylation amines
ge
st,
Dietary ab
so
protein rp
tio
n

Amino acid
degradation metabolic
Tissue protein pool

Synthesis
85%
deamination

amination of Non essential A.A NH3 α—keto acids

α—keto acids

urea oxidation Glucose, fats

other substances N.EAA

Non-essential amino acids are synthesised from the
products of their catabolism - i.e. acetyl CoA, pyruvate
or the relevant Krebs cycle intermediate. The amino
group is donated by glutamate and added by the reverse of
the transamination reactions

The essential amino acids are synthesised in micro-

organisms (bacteria and yeasts) and passed through the
food chain until they reach us in our diet. One of the
pathways essential to life which is carried out by bacteria
is the "fixation" of atmospheric nitrogen initially as
inorganic nitrate and ultimately as amino groups in amino
acids.

Higher organisms cannot perform this function.

Amino acid metabolism

 Biosynthesis of nonessential amino acids

 Catabolism
 Conversion to glucose or fat
 Urea cycle
Amino acids are absorbed in the small intestine
Amino acids are transported to the liver from the
intestines via the portal vein
In the liver, amino acids are
Used to synthesize new proteins
Converted to energy, glucose, or fat
Released to the bloodstream and transported to cells
throughout the body
Occasionally proteins are absorbed intact
Liver metabolizes amino acids, depending on bodily
needs
Most amino acids are sent into the blood to be
picked up and used by the cells
Amino acid pool is limited but has many uses
Protein turnover – the continual degradation and
synthesizing of protein
Aa.s resulting from protein digestion
are absorbed from the small intestine by:

■ passive transport mechanism (For D-aas).

■ Active transport mechanism (For L-aas and

dipeptides):
► Carrier protein transport system
( sodium – amino acid carrier system ).
► Glutathione transport system
(γ-glutamyl cycle)
 Catabolism of the a.a.s occurs by
Deamination (removal of the amino
group)
either by
General methods of deamination:
►Oxidative deamination
►Transamination
►Transdeamination
Or
Specific methods of deamination:
For certain a.a.s
 Oxidative deamination
► Definition:
It is the oxidation (removal of hydrogen) and deamination
(removal of the amino group which is liberated as free
ammonia) giving α- ketoacid and ammonia (reversible
reactions)

► Site: In most tissues , mostly in the liver and

kidney
►Site: In the cytosol or both the cytosol & the
mitochondria of most cells especially the liver

► All a.as except threonine,lysine,proline&hydroxy

proline may undergo transamination
Transamination
Urinary nitrogen excretion

LIVER
Amino acids keto acids

NH3
CO2

Urea

Blood

KIDNEY Urea

Urine
PROTEIN SYNTHESIS

Two steps:
 Transcription
Transcription involves the synthesis of an RNA transcript using the
cell's DNA as a template, leading to messenger RNA(mRNA). In
eukaryotic cells transcription happens in the nucleus.

 Translation
Once the messenger RNA is made it then is transported to the
cytoplasm where the information contained in the mRNA is
translated into a sequence of amino acids making up a
polypeptide, that will later fold into an active protein.
 
.
Biosynthesis of nonessential
amino acids
 Transamination reactions
 allow extensive interconversion between nonessential
amino acids

 requires vitamin B6 as a coenzyme

Biosynthesis of nonessential
amino acids
 From intermediates of glycolysis
 from 3-phosphoglycerate and glycine
Biosynthesis of nonessential
amino acids
 From intermediates of TCA
 From oxaloacetate
 aspartate
 amino donor in urea synthesis
 pyrimidine and purine synthesis
 asparagine
Biosynthesis of nonessential
amino acids
 From intermediates of TCA
 From α-ketoglutarate
 glutamate/glutamine
 purine and pyrimidine synthesis
 proline
 arginine
 intermediate in the urea cycle
 source of vasodilator, nitric oxide
Overview of protein synthesis
Protein Synthesis Involves Five
Stages
 Activation of amino acids
◦ Enzymatic synthesis of aminoacyl tRNA molecules
 Initiation of translation
◦ Binding of mRNA and N-formylmethionine to ribosome
 Elongation
◦ Binding of aminoacyl tRNAs to ribosome
◦ Formation of peptide bonds
 Termination and ribosome recycling
◦ Termination codon in mRNA reaches ribosome
 Folding and post-translational processing
◦ Catalyzed by a variety of enzymes
Transcription of mRNA
Translation of mRNA to make protein
 RNA contains a ribose sugar, with carbons numbered 1'
through 5'. A base is attached to the 1' position, in
general, adenine (A), cytosine (C), guanine (G), or uracil
(U). Adenine and guanine are purines, cytosine, and
uracil are pyrimidines.
DNA
Protein turnover

Catabolism
Synthesis

Amino
Gut Protein
acids

Degradation

Deposition
Protein synthesis

 On-going, semicontinuous activity in all cells but rate

varies greatly between tissues
Protein synthesis

 On-going, semicontinuous activity in all

cells but rate varies greatly between
tissues
 Rate is regulated by hormones and supply
of amino acids and energy
 Energetically expensive
 requires about 5 ATP per one peptide bond
 Accounts for about 20% of whole-body
energy expenditure
Protein degradation

 Also controlled by hormones and energy status

 Method to assist in metabolic control
 turns off enzymes
Protein synthesis and degradation

 Synthesis must exceed degradation for net protein deposition or secretion

 Changes in deposition can be achieved by different combinations of

changes in synthesis and degradation
 Other possible reasons for evolution of protein turnover include
 Allows post-translational conversion of inactive peptides to active forms (e.g.,
pepsinogen to pepsin)

 Minimizes possible negative consequences of translation errors

Changes in deposition

Synthesis Degradation Deposition

No change

No change

No change
Summary….
Protein catabolism

 Occurs when
 dietary protein exceeds requirements
 composition of absorbed amino acids is unbalanced
 gluconeogenesis is increased

 Some net catabolism of body proteins occurs at all

times
 Expressed as urinary nitrogen excretion
 yields urea
 Minimal nitrogen excretion is termed endogenous
urinary nitrogen (EUN)
Urinary nitrogen excretion

LIVER
Amino acids keto acids

NH3
CO2

Urea

Blood

KIDNEY Urea

Urine