International Journal of Advanced Research in Chemical Science (IJARCS)

Volume 3, Issue 9, September 2016, PP 1-10

ISSN 2349-039X (Print) & ISSN 2349-0403 (Online)
http://dx.doi.org/10.20431/2349-0403.0309001
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Educational Experiments about Proteins and their Properties

Mireia Díaz-Lobo*, Josep M. Fernández-Novell
Department of Biochemistry and Molecular Biomedicine,
Faculty of Biology, University of Barcelona, Barcelona, Spain

Abstract: The article shows educational experiments related to protein properties which could be easily
adapted to any educational level, from primary to high school and even University. Furthermore, each of these
experiments is about the most important properties of proteins such as stability, solubility, acid-base
precipitation and both chemical and physical denaturalization. Moreover, these didactic practicals introduce
four relevant techniques in chemistry such as isolation, purification, crystallization and osmosis. Therefore,
through them, teachers could introduce diverse relevant concepts which are normally included in the
curriculum of chemistry subject depend on the educational level. Additionally, all the educational experiments,
described in this work, could be performed in both University and school laboratories because they only need
common chemical compounds and basic materials. The main aim of the authors is to encourage science
teachers to use these educational practices as pedagogical tools to consolidate and integrate the knowledge that
students receive in theoretical classes.
Keywords: Didactic tool, practicals, protein properties, denaturalization, osmosis.

1. INTRODUCTION
Students (ages 6-18) define chemistry as one of the more complex and boring subjects in primary,
secondary and even high school [1-3]. Furthermore, students find chemistry subject really difficult to
understand, therefore they are not enough motivated and consequently some chemical concepts are
not easy to explain to them [4-7]. For these reasons, one of the most challenges in the education world
is capture student‟s attention and gives them the basic vocabulary in order that they could interpret
and discuss chemical phenomena at both adequate and acceptable level [8-10]. An effective way to
capture their attention is to perform experiments, adequate to the educational level, because students
could observe the chemical properties by themselves, and even doing these didactic experiments in
groups in order to discuss them in a pleasant atmosphere [11-12]. Moreover, working in groups also
helps students to learn how to communicate their ideas and doubts with other members of the group,
focus on solving questions and develop social skills such as teamwork, tolerance and respect for
others‟ opinions [13-15].
On top of that, there is growing interest among most scientist, science educators and teacher
community to include practical lessons and laboratory experiments as active learning approaches,
which allow students to appreciate how primary evidence is used to construct scientific knowledge.
Additionally, our teaching experiences suggest that didactic experiments are an effective pedagogical
tool to offer evidence-based science instruction to students, and, at the same time, students could
consolidate and integrate the knowledge received in theoretical classes and, besides, they could
acquire a wide and profound theoretical knowledge base [16-20].
The aim of the present contribution is to describe some laboratory experiments related to proteins and
their chemical properties using common chemical substances in order to offer teaching tools to
science teachers that allow them to introduce their students, from all educational levels, into the world
of chemistry and increase their interest in this science. These didactic experiments are about the most
important properties of proteins such as solubility, stability, acid-base precipitation and both chemical
and physical denaturalization. Furthermore, they introduce four relevant techniques in chemistry such
as isolation, purification, crystallization and osmosis. Therefore, each didactic experiment presents
different relevant concepts which are included in the curriculum of chemistry subject in Spain [21].
On one hand, these educational experiments present a high versatility because they can be adapted
perfectly to either primary, secondary, high school or University curriculum depending on the depth
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Mireia Díaz-Lobo & Josep M. Fernández-Novell

of the concepts and explanation given to students and the chemicals used to perform the practicals. On
the other hand, these experiments demand both basic and common material resources so a broad
spectrum of science teachers and academic institutions could perform them in school and University
laboratories.
2. AMINO ACIDS AND PROTEINS
Proteins are natural polymers made of amino acids. They have important functions in living systems,
for instance, they provide structural support, catalyse reactions, carry oxygen, control pH and perform
a wide range of activities in human cells. In fact, proteins are the third macronutrient essential for
living cells because each cell in everybody needs some type of protein [22].
Alpha amino acids are the monomers or building blocks in proteins. All the amino acids are similar in
structure because each has two characteristic functional groups: the amino group (-NH2) and the acid
group (-COOH). They also contain a characteristic side chain that differentiates each amino acid from
others. Depending of the nature of the side chain, the amino acids could be classified as nonpolar
(hydrophobic), polar (hydrophilic), aromatic, basic and acid amino acid (Figure 1). In nature, there are
more than 100 different types of amino acids to be found. However, human cells use only 20 of them.
About half of the amino acids (11 aa) required for building proteins could be naturally synthesized by
cells, however, the other half, called essential amino acids (9 aa), must be provided by food
supplementation. The nine essential amino acids are phenylalanine, valine, threonine, tryptophan,
methionine, leucine, isoleucine, lysine and histidine (F, V, T, W, M, L, I, K and H) [22].

Fig1. Classification of amino acids depending on the nature of their side chain
Proteins are classified in 8 groups according their functions: structural, storage, defensive, enzymatic,
hormonal, transport, receptor and contractile proteins [23].
Structural proteins, also known as fibrous proteins, provide structural support. They include collagen,
tubulin, elastin and keratin. For instance, keratin is the main structural component in hair, nails, skin,
teeth and membranes like egg membrane.
Storage proteins mainly store mineral ions, such as iron, calcium and potassium, and also amino acids
in living cells. Ferritin is an example of mineral ion storage protein which function is regulates the
amount of iron in cells. Amino acid storage proteins have a crucial role in embryonic development of
animals and plants. For instance, two amino acid storage proteins are casein and ovalbumin which are
found in milk and egg white, respectively. Concretely, casein supplies not only amino acid but also
carbohydrates and two inorganic elements which are calcium and phosphorus.
Defensive proteins are a core part of the immune systems of living beings, keeping diseases at bay.
Antibodies, or immunoglobulins, are proteins, which are formed in the white blood cells, which attack
bacteria, virus and other harmful microorganisms, rendering them inactive. Immunoglobulins are also
found in some liquids such as blood or milk. Lactoglobulins, which are the thirds most abundant
protein type in milk, carry the immunological properties of this liquid.
Enzymatic proteins accelerate metabolic processes in cells including digestion, liver functions,
converting glycogen to glucose or blood clotting. For example, digestive enzymes are the proteins that
break down food into simpler forms that the body can easily absorb. One of the enzymes involved in
glycogen metabolism is glycogen phosphorylase that catalyses the phosphorolytic cleavage of the α-
1,4 glycosidic bonds, using inorganic phosphate as co-substrate to release glucose-1-phosphate as the
reaction product.
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Educational Experiments about Proteins and their Properties

Hormonal proteins are protein-based chemicals secreted by cells of the endocrine glands and usually
transported through the blood. They act as chemical messengers transmitting signals from one cell to
another. Insulin is an example of hormone, which is secreted by pancreatic β-cells to regulate the
levels of sugar in the blood.
Transport proteins carry vital materials across cell membranes. Hemoglobin transports oxygen to
body tissues from the lugs, serum albumin carries fats in the bloodstreams and calbindin facilitates the
absorption of calcium from the intestinal walls.
Receptor proteins are located on the outer part of the cells and control the substances that enter and
leave the cells such as water, nutrients and ions.
Contractile proteins, also called motor proteins, regulate the muscle contraction and the strength and
speed of heart. Actin and myosin are two examples of this type of proteins.
As mention before, proteins are made up of many hundreds of individual amino acids and each one
may have a positive or a negative charge, depending on the pH of the system. At some pH value, all
the positive charges and all the negative charges on the protein will be in balance, so that the net
charge on the protein will be zero. That pH value is known as the isoelectric point (IEP) of the protein
and is generally the pH at which the protein is least soluble and precipitate.
Protein could be denaturalized by chemical or physical methods. The denaturalization of a protein is a
process by which the biomolecule loses its three-dimensional structure. Chemical denaturalization is
performed adding a chemical compound such as alcohol to the protein, while a physical
denaturalization is done heating (frying and boiling) or freezing at -20ºC in the fridge or at -196ºC
with liquid nitrogen [23].
2.1. Isolation of Casein, Lactalbumin and Lactoglobulin from Milk
Milk is the most nutritionally complete food in nature because of containing vitamins (principally
vitamins B1, B2, B5 and also vitamins A, B12 and D), minerals (calcium, potassium, phosphorus and
trace metals), proteins (casein, lactalbumin and lactoglobulin), carbohydrates (lactose) and lipids
(straight chain fatty acids that are saturated and have 4 to 18 carbons, monounsaturated fatty acids
[16:1, 18:1], and polyunsaturated fatty acids [18:2, 18:3]).
Casein, lactalbumin and lactoglobulin are globular proteins that fold back themselves into compact
spheroidal units, making them more easily solubilized in water as colloidal suspension than fibrous
proteins are. Moreover, they contain all the amino acids essential for living cells [24].
Casein, the principal protein of milk, is a phosphoprotein with phosphate groups attached to the
hydroxyl groups of the side chain of its amino acids. In fact, casein exists in milk as a calcium salt,
calcium caseinate, and it is formed by three similar proteins which differ from each other in their
molecular weight and the amount of phosphorus groups (α, β and κ caseins). These proteins form a
micelle which is a solubilized unit. The second most abundant protein type in milk is the lactalbumin
(albumin). Once the casein has been precipitated acidifying the solution and removed (see 2.1.1
section), the lactalbumin can be isolated by heating the mixture to precipitate it. A third type of
protein in milk is the lactoglobulin. It is present in smaller amounts than the albumin and generally
denatures and precipitates under the same conditions as the albumin. The lactoglobulin carries the
immunological properties of milk, protecting the young mammal until its own immune system has
developed [24].
2.1.1. Experimental Procedure
The following educational experiment explains not only how to isolate casein from milk, but also two
others proteins, lactalbumin and lactoglobulin.
Casein exists in milk as a calcium salt, calcium caseinate, which has its isoelectric point (neutrality) at
pH 4.8 and it is the pH value at which casein is precipitated. The pH of milk is about 6.6, therefore
casein has a negative charge at this pH and is solubilized as a salt [25-26]. If some drops of 0.1 M
chloride acid are added to milk, the negative charges on the outer surface of the micelle are
neutralized because the phosphate groups are protonated and the neutral protein precipitates: Ca2+-
caseinate + 2HCl → casein↓ + CaCl2

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Mireia Díaz-Lobo & Josep M. Fernández-Novell

The calcium ions remain in solution. The casein precipitate is a yellowish white solid (Fig 2B),
without odour and flavour, insoluble in water, but it could be resolubilized in basic and acid medium,
adding NaOH or more HCl, respectively, forming the corresponding sodium caseinate or casein
chlorohidrates (Fig 2C) [25-26]. After the isolation of casein, the milk mixture, which now is acidic,
contains the proteins lactalbumin (albumin) and lactoglobulin. When the milk mixture is heated at
75°C for 10 min, both lactalbumin and lactoglobulin are completely denaturalized and they precipitate
(Fig 2D).

Fig2. Precipitation of casein, lactalbumin and lactoglobulin. (A) Cow milk. (B) Casein is precipitated adding
some drops of 0.1M HCl (acid medium). (C) Resolubilization of casein precipitate adding NaOH or more HCl,
forming the corresponding sodium caseinate or casein chlorohidrates. (D) After the isolation of casein,
lactalbumin and lactoglobulin from milk could be precipitated heating at 75ºC during 10 min the milk mixture.
2.2. Denaturalization of Ovalbumin from Egg
There are many easy experiments that could be done with eggs, encompassing a number of different
scientific principles such as denaturalization, acid/base reactions and osmosis. The egg presents
different parts: shell, membrane, air pocket, white and yolk. The egg white is also known as the
albumen, which comes from albus, the Latin word for “white.” The main protein of egg white is
ovalbumin (albumin). The egg white also contains approximately other 40 different proteins [27].
The next experiment explains how to chemical or physical denaturalized proteins present in the whites
and yolks of raw eggs in order to obtain eggs that seems to be cooked and observe if these eggs come
back to their original states (raw) after stopping the methods of denaturalization.
2.2.1. Experimental Procedure
Three raw eggs are cracked and placed in three different bowls. In the first bowl, alcohol is added
until totally cover the raw egg (Fig 3A). In the second bowl, boiling water is added until completely
cover the raw egg (Fig 3B). In the third bowl, nitrogen liquid is carefully added until cover the raw
egg (Fig 3C). After 30 minutes, the three raw eggs seem to be cooked because egg whites lose their
transparent appearances and start to become white (Fig 3D-F). Only the second egg is really cooked
by the boiling water (Fig 3E).
When the eggs are placed in other bowls without alcohol as denaturalization agent, boiling water or
liquid nitrogen, the denaturalization processes are stopped. The eggs, which have been denaturalized
with alcohol and boiling water, do not return to its original state, in other words, to be raw (Fig 3G-
H). However, the egg, which has been frozen with liquid nitrogen, is defrosted after a couple of hours
and becomes to be raw (Fig 3I). Theses phenomena could be explained taking into account that
chemical denaturalization is normally an irreversible phenomenon but physical denaturalization could
be an irreversible phenomenon such as heat exposure (boiling or frying) or a reversible phenomenon
like cooled exposure (freezing). In the heat exposure, proteins are unfolded and covalent bounds
among chains of proteins are formed, for that reason, the alterations of the three-dimensional
structures of proteins are irreversible. While, in the cooled procedure, the molecules of waters around
the chains of proteins are frozen and their sizes are bigger than their sizes in liquid state and unfold
the three-dimensional structure of proteins. When the molecules of waters return to their liquid state,
the three-dimensional structure of proteins is refolded and their alteration is reversible [23].

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Educational Experiments about Proteins and their Properties

Fig3. Protein denaturalization. Raw eggs covered with ethanol (A), boiling water (B) and liquid nitrogen (C).
After 30 minutes, the three egg whites lose their transparent appearances and are completely white (D-E-F). 2
hours later of removing ethanol, water and nitrogen liquid, the eggs denaturalized with alcohol and boiling
water, do not return to its original state (G-H), nevertheless, the egg froze with liquid nitrogen is defrosted and
becomes to be raw (I).
2.3. Crystallization of Lysozyme from Egg White
Lysozyme is an antibacterial agent that breaks down the cell walls of some bacteria. In humans, it is
abundant in a number of secretions, such as tears, saliva and mucus. Large amounts of lysozyme can
also be found in chicken egg whites. This protein is a well-studied (monomeric enzyme of 14.4 kDa),
which can easily be purified from hen egg-white. Moreover, lysozyme was among the first proteins
that was obtained with high purity and subsequently sequenced because of its high isoelectric point.
Various salts of this small monomeric protein were crystallized early owing to both its abundance and
its stability [28-29]. In the sixties, a first 3D structure was determined at high resolution by X-ray
crystallography [30]. Since then, many crystal structures of lysozyme not only from hen and but also
other sources have been deposited with the Protein Data Bank (PDB [31]) and the Lysozyme
Structural Database (LySDB [32]). Lysozyme has the advantage to be an inexpensive biological
material. For all above reasons, it is ideal for teaching purposes. The function of a protein depends on
its three-dimensional structure because only when it is folded, the amino acids are close enough to
form an active site or a specific binding site as in the case of an enzyme or antibody, respectively.
Scientists investigate the structure of proteins to understand their functions and processes that they are
involved in life. In order to study their structure and function, scientists try to crystallize them though
of the difficulty of determining the right conditions under which each protein could crystallize.
2.3.1. Purification of Lysozyme from Hen White Egg
In this didactic experiment, either commercial lysozyme or purified lysozyme from hen white egg
could be used for crystallization. Indeed few steps are necessary in order to obtain pure lysozyme
from white egg. One fresh hen egg-white is suspended in one liter of 1M glycine pH 10. The
suspension is homogenized by stirring gently with a glass rod and later filtered through cheesecloth. A
10 mL aliquot of this preparation is carefully loaded on a CM52 cellulose ion-exchange
chromatography column (i.d. 1.5 cm, length 20 cm) that is previously washed with 5 mL of deionized
water and equilibrated with 15 mL of 1M glycine pH 10. After loading the egg preparation, the
column is then washed with 15 mL of 1 M glycine pH 10. Lysozyme is eluted with 5 mL of 0.5 M
NaCl in 1M glycine pH 10 and collected in three fractions: the first 1 mL corresponding to the void
volume of the column, the next 2 mL containing most of the pure lysozyme and the last 2 mL even
contain some pure lysozyme but in minor concentration [33]. 150 µL aliquots of pure lysozyme
fractions could be stored at -20 °C for crystallization procedure.
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Mireia Díaz-Lobo & Josep M. Fernández-Novell

2.3.2. Crystallization Procedure

Crystals grow from an aqueous protein solution, which is brought into supersaturation. Crystallization
proceeds in two phases: firstly, nucleation and, secondly, growth. After nucleation, it is important to
reach what is known as the „metastable zone‟, in which the best conditions are found for the growth of
large well-ordered crystals (Fig 4A). Actually, only two competing processes decrease the protein
concentration in the supersaturated state: (1) crystallization and (2) precipitation (Fig 4A) [34].
Lysozyme from egg white crystallize in well-shaped crystals at a protein concentration of 30-40
mg/mL in sodium acetate pH 4.5 in the presence of 1.3-1.5 M NaCl or 20% of PEG400
(poliethylenglycol of molecular weight 400 Da) at room temperature during few days [33-34].
A cylindrical plastic recipient is half partially filled with a solution of 1.4 M NaCl in 1 M sodium
acetate pH 4.5. A plastic square, which is bigger than de diameter of the cylindrical, is cut and will be
used as a cup to seal the vessel. In the cup are added 10 µL of 60 mg/mL lysozyme and 10 µL of 1.4
M NaCl in 1 M sodium acetate pH 4.5. Carefully the cylindrical vessel is sealed with the coverslip
resting the drop of protein solution inside the cylinder. It is highly recommended to close the
crystallization vessel with crystal clear sealing tape to prevent evaporation from the vessel (Fig 4B).
The crystals will start to grow in few days at room temperature. After about 1-2 weeks, crystals will
have grown to their final size (Fig 4C). The crystals are enough big to be observed by eye. A sealed
vessel will keep up to a year, sometimes even longer. The method used in this educational practice is
called “hanging drop”, which is one of the vapor diffusion methods, is the most frequently used
method in protein crystallography (Fig 4B). Since the concentration of salt ions is higher in the
crystallization solution (reservoir) than in the mixture on the hanging drop, solvent molecules will
move from the protein drop to the reservoir by vapor diffusion in the gas phase. During this process,
the solubility of the protein in the drop decreases. The protein solution in the drop finally becomes
supersaturated, which is a thermodynamically unstable state. This causes some of the protein in the
drop either to form crystal nuclei that finally grow into larger protein crystals (Fig 4C), or to
precipitate as amorphous protein which is useless for X-ray analysis. It is extremely important to find
the optimal conditions favoring crystallization because crystallization and precipitation are two
competing processes (Fig 4A).

Fig4. Crystallization of lysozyme from white egg. (A) Diagram of the different zones in crystallization
proceeds. (B) Scheme of vapor diffusion method. (C) Crystals of lysozyme which are formatted and growth in
1M ammonium acetate pH 4.5 with 1.4 M NaCl at room temperature after 2 weeks.
2.4. Studies of the Properties of Egg Membrane
The following didactic experiment describes the effects of acids on an eggshell (acid-base reaction),
the obtainment of naked egg and the study of the selectively permeability of egg membrane in front of
different types of solutions (osmosis).
2.4.1. Acid-Base Reaction in the Eggshell
When an egg is submerged in vinegar, the eggshell is dissolved leaving the inner semi-permeable
membrane intact. In fact, the acetic acid of the vinegar reacts with the solid calcium carbonate crystals
(base) of the eggshell breaking apart the calcium carbonate into their calcium and carbonate ions:
CH3COOH (aq) + CaCO3 (s) → Ca2+ (aq) + CH3COO- (aq) + H2O (aq) + CO2 (g) ↑
While the calcium ions stay dissolved in the vinegar, the carbonic acid formed during the reaction is
an unstable weak acid that quickly decomposes into water and carbon dioxide. For that reason, when
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Educational Experiments about Proteins and their Properties

the acetic acid of vinegar dissolves the calcium carbonate, a strong detachment of bubbles of carbon
dioxide is observed (Fig 5A). In order to dissolve completely the eggshell, the egg should be in
vinegar at least 48h at room temperature. After this time, the naked egg (shell-less egg) should be
carefully washed with water. It is important to point out that the egg membrane is the only thing
holding the egg together and it is not as durable as the shell. To conserve the egg membrane, the
naked egg should be placed back in fresh vinegar and keep in the fridge.
In addition, the egg without a shell looks like an egg, but it is translucent, the membrane flexes when
it is gently squeezed (Fig 5B) and is bigger than before. Some of the vinegar permeates the egg
membrane, which is why the egg swells (osmosis, for an explanation see 2.4.2). If a raw egg is boiled,
it is easy to compare the size of this egg with the size of the naked egg and observe how the naked egg
swells during the experiment (Fig 5C). When the naked egg is carefully shacked, the yolk sloshes
around in the white. If the membrane tears, the contents that will spill out are just the same as any raw
egg, with only the difference of having some vinegar (Fig 5D).

Fig5. Obtainment of a naked egg. (A) Acid acetic of vinegar dissolves the solid calcium carbonate crystals of
the egg shell. (B) The naked egg is translucent and flexes when it is gently pressed. (C) The egg swells because
some the vinegar permeates the egg membrane. This fact is easy to observe if a hard-boiled egg is placed near a
naked egg.(D)If the membrane of a naked egg is teared, we could observed that the yolk and the white still raw.
2.4.2. Osmosis with Eggs
After dissolving the eggshell, the membrane is the only component that holds the insides of the egg.
This membrane is selectively permeable because allows some molecules move through it and blocks
out other molecules [35]. For instance, water moves through the membrane easily, while bigger
molecules such as sugars or proteins do not pass through it. Due to the selectively permeability of the
egg membrane, several educational experiments could be perform with naked eggs in order to study
the process of osmosis. Concretely, osmosis is a process in which water moves through a membrane
[36]. The natural movement of water is from the side of the membrane with a high concentration of
water to the side with a low concentration of water. The term osmosis only refers to water, while
diffusion refers to all other substances spreading from a higher concentration to a lower concentration
[36]. As mention above, the egg expanded in the vinegar solution, when its shell is dissolved, because
the vinegar has a higher concentration of water (94%) than the inside of the egg (90%) [27].
Therefore, water molecules move from the vinegar into the egg through the semi-permeable
membrane so as to reach the equilibrium. If the membrane were completely permeable, water
molecules would move into the egg as well as protein would move out the egg until both solutions
were the same concentration. Since the egg membrane is semi-permeable, water can move in but
proteins cannot move out. On the other hand, a naked egg into water coloured with food colouring
swells significantly. The coloured solution has a concentration of water (>99%) higher than the egg
(90%). To reach the equilibrium, the water molecules migrate inside the egg, leaving it plump and
firm (Fig 6A).
Moreover, when naked egg is placed in glucose syrup the egg shrinks due also to osmosis, but in the
opposite direction than happens with vinegar. Syrup is mostly sugar, thus, its concentration of water
(25%) is lower than the egg (90%). Osmosis causes the water molecules move from the side of the
membrane where they are more abundant to the side where they are less abundant. So water migrates
from inside to outside the egg, into the glucose syrup until both solutions have the same concentration
of water. The outward movement of water leaves the egg limp and flabby (Figure 6C). Furthermore, if
a naked egg is in salty water, the egg shrivels too because of the outward movement of water.
Nevertheless, not only water passes through the membrane and go inside the egg, colorant also moves
in, giving the egg a dark orange colour (Fig 6A). Due to the high concentration of glucose that has
syrup, glucose molecules move in the egg giving it a brown colour (Fig 6C). The raw egg, treated
with aqueous red cabbage extract, has a violet colour because anthocyanin molecules of the extract
move in the egg and in contact with egg white, which is slightly basic (pH 7.6-8.0), become bluish
violet (Fig 6E).
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Mireia Díaz-Lobo & Josep M. Fernández-Novell

Fig6. Osmosis results in naked egg. Naked egg treated with colorant (A), naked egg without treatment used as
control (B), naked egg treated with dark syrup (C), hard-boiled egg (D) and naked egg treated with aqueous red
cabbage extract (E). Same eggs mentioned above which are observed thought a bulb light, all the naked eggs
are translucid, except the hard-boiled egg, indicating that naked eggs are indeed raw eggs.
3. CONCLUSION
These experiments can be related, according to educational level, with: the principle properties of
proteins such as solubility, stability, acid-base precipitation and both chemical and physical
denaturalization. Moreover, these didactic experiments present four relevant techniques in chemistry
such as isolation, purification, crystallization and osmosis. Furthermore, most of these experiments
can be done using both basic equipment and chemicals found in a normal laboratory, helping science
teachers perform experiments that have all the characteristics of excellent classroom demonstrations
because of their high degree of safety, ready availability of materials, visual interest and relative
simplicity.
The benefits of using practical experiments as educational tools are diverse. When science teacher
explain experiments and help students to perform it, not only do students gain confidence in their
ability, but also improve their understanding of theoretical knowledge through experimentation [37-
39]. Besides, each experiment becomes clear for students because scientific concepts and techniques
are gradually introduced by their teachers. By the end of practical lessons, students are capable of
discussing the experiments logically and critically, generating valid conclusions, and also applying the
scientific methods and techniques they learn to hypothetical situations involving scientific research.
Science teachers could also show students how to identify hypotheses from the educational practices,
explore the experimental methodologies used and analyze the data. Moreover, through these
practicals, science teachers could demonstrate to students the importance of using safety personnel
equipment and useful information on substance safe handling. Additionally, if science teachers do
experiments in groups, students could develop soft skills such as problem solving, teamwork and
communications, which are essential skills in the students‟ future [40-42]. Theoretically lessons
essentially test the ability to memorize facts, while educational practices test the capability to
formulate new hypotheses, suggest experiments and propose future directions for the research [43].
On the other hand, a way that science teachers have to increase knowledge of chemistry among
students is to include educational practice in their routine. Authors strongly defend that a good
chemistry education provides students with not only valuable theoretical and experimental concepts
but also life skills and career options.
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