Proteins are essential nutrients for the human body.

They are one

of the building blocks of body tissue, and can also serve as a fuel source.
As a fuel, proteins provide as much energy density as carbohydrates:
4 kcal (17 kJ) per gram; in contrast, lipids provide 9 kcal (37 kJ) per gram.
The most important aspect and defining characteristic of protein from a
nutritional standpoint is its amino acidcomposition.
Proteins are polymer chains made of amino acids linked together
by peptide bonds. During human digestion, proteins are broken down in
the

stomach

to

smaller polypeptide

chains via hydrochloric

acid and protease actions. This is crucial for the synthesis of the essential
amino acids that cannot be biosynthesized by the body.
There are nine essential amino acids which humans must obtain
from their diet in order to prevent protein-energy malnutrition. They are
phenyl
alanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysi
ne, and histidine. There are five dispensable amino acids which humans
are able to synthesize in the body. These five are alanine, aspartic
acid, asparagine, glutamic acid and serine. There are six conditionally
essential amino acids whose synthesis can be limited under special
pathophysiological conditions, such as prematurity in the infant or
individuals

in

severe

catabolic

distress.

These

six

are arginine, cysteine, glycine, glutamine, proline andtyrosine.

Humans need the essential amino acids in certain ratios. Some
protein sources contain amino acids in a more or less 'complete' sense.
This has given rise to various ranking systems for protein sources, as
described

in

the

article.

Sources

of

protein

include grains, legumes and nuts, as well as animal sources such as

meats, dairy products, fish and eggs. Vegetariansand vegans can get
enough essential amino acids by eating a variety of plant proteins. It is
commonly believed that athletes should consume a higher-than-normal

protein intake to maintain optimal physical performance. How to classify

the amino acids there are several ways including fundamental way on the
number of carboxylic groups and groups of amino acids contained by the
compound. (Bayu. D, 2002)
All amino acids, or peptides containing free amino will react with
ninhydrin to form a complex compound of blue-purple. However, proline
and hidroksipolin produce yellow compound. (Berry, S, 2000).
Proteins are amphoteric, which can react with acidic or alkaline
solution. Different protein solubility in water, acid and alkaline soluble
portion there, and some are difficult sea. If the proteins are not soluble in
fat such as ether or chloroform. If the protein is heated or added absolute
ethanol then menggumpul proteins (coagulated). This is due to the
ethanol mental attract water molecules that complement proteins.
Egg
Eggs are one of the foods of high nutritional value because it
contains nutrients that are needed by the human body such as fat,
protein, vitamins and minerals, and has a high digestibility (Sirait, 1986).
Number of albumen in the circle intact eggs is about 60%, contains five
types of protein and less carbohydrates. Albumen or egg white is
commonly called a globular protein which is not tight or arranged in a
certain order. Water molecules easily break into empty spaces in the
protein molecule. Globular protein can be dispersed well in water or saline
solution, to form a colloidal, and are affected by acid, alkali and heat
(Gaman and Sherrington, 1992). Rasyaf (1985) stated that there are five
types of proteins in the egg white ovalbumin, ovomukoid, ovomusin,
ovokoalbumin, and ovoglobulin. Fresh egg white protein is seen as a
system consisting of fiber aquaeus ovomucin in a solution that contains a
lot of protein. Ovomucin, with a carbohydrate content of about 10%, is the
most common protein found in the middle layer of albumen. Ovomucin
only soluble in an alkaline solution.

Milk
Milk is a nutritious white liquid produced by the mammary glands of
mammals and humans. Milk is the primary source of nutrition for babies
before they can digest solid food. Today, the milk has many functions and
benefits. For the productive age, milk helps their growth. Meanwhile, for
the elderly, milk helps sustain bone so that it is not porous. Milk naturally
contains essential nutrients, such as an assortment of vitamins, protein,
calcium, magnesium, phosphorus, and zinc, another added that milk
contains minerals and fats. Hence, everyone is encouraged to drink milk.
The composition of milk of which consists of water, dry matter, fat, nonfat
dry matter, protein, and lactose. Each animal has a composition of milk
varies, both among animals, among species, and between the nations of
animals. Cow's milk has a fat content of 3.1%, 2.8% protein, 11.2% dry
matter, dry matter without fat 8.1%. While goat milk composition
consisting of 6.34% fat, 4.97% protein, dry matter 15.32%, nonfat dry
matter 8.97%. Based on the results of the composition, it can be
concluded that dry matter, fat, and protein goat milk is higher than in
cow's milk.

Protein Denaturation
Protein denaturation can be interpreted a change or modification to
the structure of secondary, tertiary and quaternary protein molecule
without breaking the bonds kovelen. Therefore, denaturation can mean a
process of breaking up the hydrogen bonds, hydrophobic interactions, salt
ties and the opening of the pleat folds or protein molecules.
Denatured protein will be reduced solubility. Molecular layer in the
hydrophobic part will be out while the hydrophilic part will be folded into.
Folding or pembakikkan will occur when the protein approached isoelektris
pH and protein will clump and settle. Viscosity increase due to expand into
asymmetric molecules, optical rotation angles protein solution will also
increase.

Protein denaturation include disruption and damage that may occur

in the secondary and tertiary structure of proteins. Since it is known
denaturation reaction was not strong enough to break the peptide bond, in
which the primary structure of proteins remain the same after the
denaturation process. Denaturation occurs due to a disturbance in the
secondary and tertiary structure of proteins.
At the tertiary protein structure, there are four types of interactions
that form a bond in the side chain such as; hydrogen bonding, salt bridge,
disulfide bond and non-polar hydrophobic interactions, which may be
impaired.

Denaturation

commonly

encountered

is

the

process

of

precipitation and coagulation of proteins.

a. Denaturation due to heat
Heat can be used to disrupt the hydrogen bonds and
hydrophobic interactions nonpolar. This happens because the high
temperatures can increase the kinetic energy and cause the building
blocks of protein molecules move or vibrate so fast that disrupt the
molecular bonds. Egg proteins undergo denaturation and coagulated
during cooking. Some of the food is cooked to denature the proteins
contained in order to facilitate the digestive enzymes to digest the
protein.
Warming will make denatured protein material so the water
binding capability decreases. This happens because the heat energy
will result in the dissolution of non-covalent interactions that exist in
the natural structure of proteins but does not break covalent bonds
that form peptide bonds. This process usually takes place in a
narrow temperature range.
Alcohol can also damage the hydrogen bonds. Hydrogen
bonding occurred between amide groups in the secondary structure
of proteins. The hydrogen bond between the side chains occurring in
the tertiary structure of proteins with various combinations of
constituent amino acids.

b. Denaturation because of acid and base

Protein will experience the greatest turbidity when it reaches
ph ph isoelektris ie which protein has a positive and negative charge
the same, at the time
marked proteins undergo
denaturation
increased

turbidity
and

the

incidence of clots. Acids and bases can disrupt the salt bridges in
the presence of ionic charge. A type of double displacement reaction
occurs when positive and negative ions in the salt change partners
with positive and negative ions derived from an acid or base is
added. This reaction occurs in the digestive system, when stomach
acid mengkoagulasi milk consumed.

c. Denaturation for heavy metal salts:

Heavy metal salts denature the protein the same as well as
acids and bases. Heavy metal salts generally contains Hg+2, Pb+2,
Ag+1 Tl+1, Cd+2 and other metals with large atomic weight. The
reaction that occurs between heavy metal salt will result in the
formation of protein-metal salts that are not soluble.
Protein will experience precipitation when it reacts with metal
ions. By deposition of positive ions (metal) required above solution
ph pi because negatively charged protein, precipitation by negative
ions required under the solution ph pi because protein is positively
charged. The positive ions that can precipitate proteins are; Hg+2,
Pb+2, Ag+1 Tl+1, Cd+2 while the negative ions that can precipitate
proteins are; salicylate ion, triklorasetat, piktrat, tannic and
sulfosalisilat.
The presence of heavy metal salts can also damage disulfide
bonds, because affinitasnya high and its ability to attract sulfur

resulting in protein denaturation. Disulfide bonds formed by the

oxidation of sulfhydryl groups on cysteine. Between different
protein chains which together have a sulfhydryl group will form
covalent
bonds
strong.

disulfide
are

very

Reducing

agents may decide

disulfide bonds, where the addition of hydrogen atoms to form a
thiol group; -SH.
Denatured protein will be reduced solubility. Layers of protein
molecules in the hydrophobic part will be out, while the hydrophilic
portion to be folded into. Folding or reversal occurs when the
protein solution approaching pH isoelectric, then proteins would
clump and settle. The viscosity will increase because the molecules
expand and become asymmetric, optical rotation angles protein
solution will also increase. Protein denaturation can be caused by
heat, pH, chemical, mechanical and others.
Protein will experience the greatest turbidity when it reaches
ph isoelectric is pH where protein has a positive and negative
charge

the

same,

at

the

time

marked

proteins

undergo

denaturation turbidity increased and the incidence of clots. Various

globular proteins have a different solubility in water. Variables that
affect solubility are: pH, ionic strength, dielectric properties of the
solvent, and temperature. The separation of protein from the
mixture with a pH adjustment is based on the pH-isoelectric
different for each type of protein. In general, the solubility of the
protein molecule has a minimum at the isoelectric pH. At some
protein isoelectric pH will precipitate out of solution. So by way of
adjusting the pH of the solution, each of the proteins in the mixture
can be separated one from another by a technique called isoelectric
precipitation.
The addition of alkali compounds in protein leads to
hydrolysis of the polymer protein. hydrolisis peptide monomers

produces amino acids and some amino and partial amino group
that turns into ammonia.
Color Reaction of Protein
a. Biuret Reaction
Biuret reaction is a reaction common color for cluster peptide (CO-NH-) and protein. A positive reaction characterized by the
formation of purple for the complex compounds are formed between
Cu2 + and N of the molecule peptide bond. The number of amino
acids bound to the peptide bond affects the color of this reaction.
Compounds with dipeptide gave blue, purple and tripeptide and
tripeptide peptide complex gives a red color. Some proteins have a
group -CS-NH-, CH-NH- in the molecule also provide a color test
positive biuret reaction to form a complex compound.
b. Reaksi Ksanthoprotein
Ksanthoprotein color reaction can occur because the nitration
reaction on the benzene ring of aminoa acid building blocks of
protein. Test positive say is indicated by the yellow color due to the
formation of a compound polinitrobenzena. The positive reaction to
a protein that contains the amino acid tyrosine to the core, for
example benzene, fnil Worlds, triftofan ,. In addition of alkaline
compounds yellow color will disappear and turn into yellow to
orange due to the nature of the acidity of the phenols react with
alkali. The orange color when acidified will turn back to yellow.
c. Ninhydrin reaction
Ninhydrin protein color reactions were positive when giving
blue or purple. This reaction occurs in the free amino group of the
amino acid with ninhirin. Blue-purple color above can also be used
to determine the amino acid quantitatively by measuring the
absorbance at 570 nm. The basic reaction used in the tools for the
determination of amino acids.

Struktur
ninhidrin:
(2,2Dihydroxyindane1,3-dione)

d. Millon reaction
Reagent millon involves adding Hg compounds into protein so
that the addition of this metal will be resulting in a white precipitate
of mercury compounds. For protein-containing tyrosine or triftofan
millon reagent additions resulting in red. However, this reagent is
not specific because it also gives a positive test with their red
phenol compound.
e. Hopkins-Cole Reaction
This protein color reaction indicates a positive signaled the
formation of the purple rings on the boundary between the protein
solution with reagents. The formation of these rings due to the
formation of condensation of two indole nucleus of tryptophan with
aldehydes. The aldehyde obtained here glioksalat acid used for testhopkins Adamkiewicz.
Hydrolysis Protein
The addition of alkali in protein can cause hydrolysis of peptide
bonds of protein polymer. This hydrolysis produces amino acid monomers
and some amino groups are transformed into ammonia. By hydrolysis of
the reduced number of amino groups. If the protein are amino acids that
have a S atom such as Cistein and Cistin in the molecule, the amino acid
can be eliminated in a compound form H2S. penambhan Pb in alkaline
salts to precipitate PbS are easily observed.
Pb2+ + 4OHPbO22- + 2H2O
S2- + 2H2O + PbO22- PbS + 4OH-

DAFTAR PUSTAKA
Abdi, 2001. Konsep- konsep Dasar Biolcimia . Bandung: Departemen P
dan K.
Anwar A. 2004. Pengantar Praktikum Kimia Organik. Yogyakarta :
Depdikbud dirjen Pendidikan Tinggi.
Bayu. D, 2002. Dasar- dasar Dalam Memahami Biokimia. Semarang:
Departemen
Pendidikan

Pendidikan
Tinggi

dan

Proyek

Kebudayaan
Pembinaan

Direktorat

Tenaga

Jenderal

Kependidikan

Perguruan Tinggi.
Berry. S, 2000. Dasar Kimia SMU III. Jakarta: PT. GramediaPustaka Utama.
Fessenden & Fessenden. 1982. Kimia Organik. Jilid 2. Edisi 3. Oleh Aloysius
Hadyana P. Kramat, Jakarta : Erlangga.
Lehninger, Albert. 1982. Dasar-Dasar Biokimia. Jilid 1. Oleh Maggy
Thenawijaya. Ciracas, Jakarta: Erlangga.