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Complete report of Organic Chemistry II with title “Amino Acid and

Protein” by:
Name : Nana Nursana Ahda
Student ID : 200105512001
Class : ICP of Education Chemistry
Group : I (One)
has been checked and revised by Assistant and Assistant Coordinator, so this
report considered accepted.

Makassar, Oktober 2021

Assistant Coordinator Assistant

Nur Rahma Amar S.pd. Fikri Munafri

ID: 1713041006aaa

Known by
Responsible Lecturer

Hardin, S.Si, S.Pd, M.Pd

NIP. 19870807 201504 1 004
A. Title of Experiment
Amino Acid and Protein
B. Objective of Experiment
Before the experiment, student have to understand the structure of protein, in
the experiment can be expected:
1. Can prove the existence of peptide bond.
2. Can understand the reaction of Xanthoproteate and lowred test to various
contents of protein.
3. Understand the solubility and the properties of the amphoter of amino acid.
4. Proficient in the way amino acids separations by paper chromatography and
their identification.
C. Literature Review
The amino acids found in proteins are -aminocarboxylic acids. Amino acids
contain an amino (-NH2) and a carboxylic (-COOH) group. The structure of an
amino acid can be described as below with variations in the structure of these
monomers occurring in the side chain (R).

general structure of amino acids .

Amino acids contain an amino group in the form of an ammonium cation and a
carboxyl group in the form of a carboxylate anion. Thus, amino acids contain
basic and acidic groups in the same molecule. An amino acid undergoes an
internal acid-base reaction to produce a dipolar ion, also called a zwitter. Because
of this structure, amino acids do not always behave like organic compounds.
Amino acids have a high melting point (200 0C), are insoluble organic solvents,
soluble in polar solvents (Wardiah, 2016 : 190).
Based on their chemical properties, amino acids are grouped into: a) amino
acids with open carbon bonds, b) basic amino acids, c) acidic amino acids, d)
amino acids with closed carbon bonds, e) aromatic amino acids. , and f) amino
acids containing sulfur ions (Suprayitno, Titik 2017 : 2).
Amino acids, in general, are combinations of ligands or hydrophilic,
hydrophobic, and ionic structural features. However, this depends on the specific
amino acid, as some are more polar than others, or charged. Amino acids are
zwitterionic, similar to peptides and proteins, they can exist as an overall neutral
form, a weak acid or a weak base, depending on the pH conditions. In addition,
each amino acid differs slightly from its neighbors at a certain pH or mobile phase
composition, which makes it quite easy to solve them, one over the other, by
carefully selecting the stationary and mobile phases (Periat, dkk 2014 : 4).
Amino acids containing carboxyl side bonds are classified as acidic amino
acids, while amino acids containing amino side bonds are classified as basic
amino acids, the rest of these two groups are referred to as neutral amino acids.
The acidic amino acids are glutamic acid and aspartic acid, the basic amino acids
are lysine, histidine, and arginine (Wardiah, 2016 : 192).
Amphoteric Amino Acids, An amino acid can react with acids or bases, each
will produce a cation or an anion. In an acidic solution, an amino acid will be
basic which will accept a proton so that it will produce a cation. In a basic
solution, amino acids will be acidic which will donate a proton so that it will
produce an anion.
 (Wardiah, 2016 : 193).

Amino acid analysis is very important, because the protein quality of a food is
largely determined by the amino acid content it contains. In terms of nutrition,
amino acids are divided into 2 groups, namely non-essential amino acids and
essential amino acids. Non-essential amino acids are amino acids that can be
provided by the organism's body through a complex biosynthetic process from
nitrogen compounds found in food, and essential amino acids are amino acids that
cannot be synthesized by the body (Elfita 2014 : 33).
Amino acids as the monomers that make up proteins (polypeptides), generally
have a central carbon atom (Cα) that binds a hydrogen atom, an amino group
(NH2), and a carboxyl group (COOH). There are 20 types of amino acids that
make up proteins, which are distinguished by side chains attached to Cα through
their fourth valence. Amino acids are connected end to end during protein
synthesis by the formation of a polypeptide bond when the carboxyl group of one
amino acid joins with the group of the next amino acid by removing water. This
process is repeated as the chain length increases. The amino group on the first
amino acid in a polypeptide chain and the carboxyl group on the last amino acid
remain intact (Rizkiyanti,dkk 2016 : 59).
Amino acids can form a bond called a peptide bond. The peptide chain is
composed of : (a) two residues of an amino acid unit called a dipeptide; (b) three
residues of an amino acid unit called a tripeptide; (c) four residues of an amino
acid unit called a tentrapeptide; (d) five residues of an amino acid unit called a
pentapeptide; (e) six residues of an amino acid unit called a hexapeptide; (f)
amino acids are called polypeptides (Saraswati 2018 : 4).
 Peptides and proteins are polymers formed from amino acid units through
peptide bonds between an -amino group of one amino acid and a carboxyl group
of another amino acid. This peptide bond will form an amide group. The amino
acids that make up the peptide are referred to as residues. An example of a peptide
formed from glycine and serine is called glycylserine (Wardiah, 2016 : 194).
Tripeptides can form combined combinations of amino acids in six ways. So
the more amino acid residues that make up the peptide, the more possible
combinations of these amino acids. Peptide names start with the amino acid
names from left to right, Examples of peptides:

(Wardiah, 2016 : 194).

Peptides (polypeptides) and proteins are almost the same and almost similar
but have what differences distinguish peptides (polypeptides) from proteins?
polypeptides and proteins are polyamides, they are the same. It's just that
polyamides with less than 50 amino acid residues are known as peptides, while
those with more referred to as proteins (Wardiah, 2016 : 194).
The term protein comes from the Greek word proteos, which means main or
precedence. This word was introduced by the Dutch chemist, Gerardus Mulder.
He argued that protein was the most important substance in every organism.
Protein is series of amino acids with peptide bonds. Three-fourths of the body's
solid substances of protein (muscle, enzymes, plasma proteins, antibodies,
hormones) (Suprayitno, Titik 2017 : 15).
Protein is a polypeptide composed of many acids is a very vital molecule for
organisms that is found in all cells. Amino acid chains are linked by specific
covalent bonds. The structure and function of proteins are determined by the
combination, number, and sequence of amino acids. The physical and chemical
properties of amino acids are influenced by the constituent amino acids. Proteins
in the body are grouped based on the tasks and functions of these proteins. These
protein groups are fiber proteins, globular proteins (Wardiah, 2016 : 195).
The stability of the protein structure is generally maintained by two types of
strong deep covalent bonds (peptide and sulfide) and three types of weak non-
covalent bonds (hydrogen, hydrophobic and electrostatic). In large protein
molecules, cysteine bonds (sulphide bonds), electrostatic bonds (salt bonds).
Hydrogen bonds and hydrophobic interactions are not only present in one
polypeptide bond but can also link one polypeptide bond with another polypeptide
bond (Saraswati 2018 : 6).
Proteins are molecules of alpha-amino acids with complex structures and
molecular weights ranging from 5,000 to several million. Based on its structure,
proteins are divided into four primary secondary tertiary and quaternary structures
(Saraswati 2018 : 6).
Because of the presence of one polypeptide bond with another polypeptide
bond that is connected by certain bonds. The bonds that contain protein molecules
are peptide bonds, cystine bonds, salt bonds, ester bonds, and hydrogen bonds.
Peptide bonds are bonds between one amino acid and another. because this bond
is present in a peptide bond, this bond is always present in a protein molecule, the
number of peptide bonds in a protein molecule can be tested by using the biuret
test (Saraswati 2018 : 8).
Proteins can undergo denaturation which results in the loss of biological
properties of the protein. Denaturation is the breakdown of hydrogen bonds and
other secondary forces in proteins, causing the loss of higher structural properties.
Factors that cause denaturation include: changes in temperature, changes in pH,
detergents, radiation, oxidizing or reducing agents. But Denaturation can be
reversible if the denaturation conditions are gentle such as a slight change in pH.
If these proteins are returned to their natural environment, they can be regain its
natural higher structure in a process called renaturation. But generally this
renaturation is very slow and does not occur at all (Wardiah, 2016 : 197).
 Reliable separation of peptides, amino acids and proteins as accurate as
possible with the maximum conformation and biological activity is crucial and
essential for drug discovery. Polysaccharide, as one of the most abundant natural
biopolymers with optical activity on earth, is easy to be functionalized due to lots
of hydroxyl groups on glucose units. Over the last few decades, polysaccharide
derivatives are gradually employed as effective separation media. The highly-
ordered helical structure contributes to complex, diverse molecular recognition
ability, allowing polysaccharide derivatives to selectively interact with different
analytes (Fan, Lilong, dkk 2021 : 1).

D. Apparatus And Chemicals

1. Apparatus
a. Measuring cup 10 mL ( 3 pieces)
b. Measuring cup 100 mL ( 1 piece)
c. Test tube ( 8 pieces)
d. Test tube racks ( 2 piece)
e. Beaker 100 mL ( 2 piece)
f. Beaker 200 mL ( 1 piece)
g. Spray bottle ( 1 piece)
h. Asbestos gauze ( 1 piece)
i. Spiritus burner (1 piece)
j. Funnel ( 1 piece)
k. Drop pipette (4 piece)
l. Tripod (1 piece)
m. Porcelain cup (2 piece)
n. Soft rag (1 piece)
o. Rough rag (1 piece)
2. Chemicals
a. Hydrochloric acid solution (HCl) 10%
b. Hydrochloric acid solution (HCl) 20%
 c. Sodium nitrous solution (NaNO2) 5%
d. Copper (II) sulphate solution (CuSO4)
e. Aquadest (H2O)(l)
f. Nitric acid concentrated (HNO3)
g. Glycine (C2H5O2N)
h. Gycine solution (C2H5O2N) 0,1 M
i. Tyrocine (C9H11O3N)
j. Casein (C18H122O6N)
k. L-aspartic (C3H6O2N) 0,1 M
l. Sodium Hydroxide solution (NaOH) 10%
m. Urea (NH2)2CO
n. Ice cube (H2O)(s)
o. Litmus paper
p. Aluminium foil
q. Label
r. Matches
s. Filter paper
E. Work Procedure
1. Solubility and amphoteric properties
a. Crystalline glycine, L-Aspartate and L-Tyrosine
1) Putting 0.1 grams of glycine crystals into 2 mL of distilled water.
2) Putting litmus paper into a mixture of glycine crystals with distilled
water.
3) Putting 0.1 grams of L-Aspartate crystals to 2 mL of distilled water.
4) Putting litmus paper into a mixture of L-Aspartate crystals with
aquades.
5) Putting 0.1 grams of L-Tyrosine crystals into 2 mL of distilled water.
6) Putting litmus paper into a mixture of L-Tyrosine crystals with
distilled water.
b. Puts 1 mL of 10% NaOH solution into 0.1 g L-Thyrosine.
c. Adds 2 mL of water, then records the results.
 d. Putting litmus paper into the solution.
e. Adds HCl drop by drop.
f. Stirring for 1 minute.
g. Adds 10% HCl and then observes.
h. Puts 0.1 g of casein into a test tube.
i. Added 5 mL of distilled water and 2 mL of 10% NaOH solution.
j. Closes the test tube and shakes it until a colloid is formed.
k. Saves 2 mL for the next experiment.
2. Reaction with nitric acid
a. Puts 0.1 g of glycine into a test tube.
b. Adds 5 mL of 10% HCl.
c. Puts 5 mL of 10% HCl in another tube.
d. Cooling these two test tubes into ice water.
e. Then the practitioner puts 1 mL of 5% NaNO2 each into the two test
tubes.
f. Puts the casein that has been obtained into the ice water.
g. Adds mL of NaNO2. and Records the results.
3. Biuret test
a. Putting 0.5 g of urea into a test tube.
b. Heats the urea until it forms gas and melts.
c. Records the smell of gas and tests it with litmus paper.
d. Continues the preparation until the gas formation stops and starts to
solidify.
e. Cooling urea solids.
f. Dissolves solid urea with hot distilled water.
g. Filters the solution and adds 2 mL of 10% NaOH into the filtrate.
h. Adds 2-3 drops of 2% CuSO4.
i. Then stirring and paying attention to the colors.
j. Dissolves 0.5 g of urea with 3 mL of water in another container as a
comparison.
k. Adds 2 mL of 10% NaOH.
 l. Adds 2-3 drops of 2% CuSO4.
m. Compares the first result with the second.
n. Mixes 2 mL of casein solution which has been provided with 2 mL of
distilled water.
o. The practitioner adds 2 drops of 2% CuSO4. Then stirs and observes.
4. Xanthoproteat test
a. Put 0.1 g of casein into a test tube.
b. Carefully adds 2 mL of concentrated HNO3. and observing colors.
c. The practitioner cools the reaction mixture, then carefully neutralizes it
with 10% NaOH solution.
d. Adding a little extra base.
e. Then note the change in the color of the solution.
5. Hydrolisis test
a. Puts 0.5 g of casein into the flask and adds 20 mL of 20% HCl solution.
Then add some boiling stones
b. Doing reflux for 10 minutes.
c. Cooling the mixture to room temperature. Then divide by 2 parts
d. Cooling some (5 mL) in ice water.
e. Compares the results with the mixture at room temperature.
f. Neutralizes with 10% NaOH.
g. Adds 3 mL of 10% NaOH solution.
h. Adds 2 drops of 2% CuSO4 solution and then heats it in a water bath.
i. Compares the results with the experiment
F. OBSERVATIO RESULT

NO ACTIVITY RESULT

1. Solution and amphoteric

properties
a). Glysin crystal + 2 mL H2O Soluble in water ( colorless)
+ litmus paper test Blue litmus Red litmus
b). L-Tyrocin 0,1 gr + 2mL H2O Low soluble in water ( turbid)
+ litmus paper test Blue litmus Blue litmus

c). L-Aspartic 0,1 gr + 2mL H2O Insoluble in water ( there are

sedimet)
+ litmus paper test Blue litmus Red litmus

d). L-Tyrocin 0,1 gr + 2mL H2O White solution

+ 1 mL NaOH 10% Colorless solution
+ Red litmus Change into blue litmus
+ HCl 10% Turbid solution
+ Blue litmus Changes into red litmus

e). Casein 0,1 gr + 2mL H2O Turbid solution

+ 1 mL NaOH 10% Colourless with white
sediment
2. Reaction with nitric acids

1 it tube
0,1 gram glycin + 5 mL HCl 10% Colourless solution
Chill the solution Colourless solution
Solution + 1 mL NaNO2 5% There are many bubbles
2 nd tube
5 mL HCl 10% and chill + 1 mL Colourless solution
NaNO2 5% Colourless and little bubble
3 nd tube
2 mL casein + chill + 1 mL Turbid solution
NaNO2 5%
3. Biuret test

0,5 urea (heated) Smelly solution

Let the solution + solution Colour white solution
dissolved in hot water + filtered + Colourles solution Deep pink
NaOH 2 mL + CuSO4 3 drops
As comparing
b). 0,5 gr urea + 3 mL H2O + 2 mL Blue solution
NaOH 10% + CuSO4 3 drops Purple solution
2 mL casein + 2 mL H2O + 2 Purple solution
drops CuSO4
4. Xanthoproteate

a). 0,1 gr casein + 2 mL HNO 3 Yellow solution and orange

concentrated heated the solution + sediment (in top solution)
NaOH 10% Yellow solution.
 5. Protein hydrolisis

0,5 gram casein + 5 mL HCl 20% Turbid solution

+ 3 boiling stone heated solution
23 minute and chill in ice water + Brown solution
3 mL NaOH 10% + 3 drops Brown solution (no changes)
CuSO4 2%
Heated the solution Light solution (light solution)
0,5 gram casein + 5 mL HCl 20% Turbid solution
+ 3 boiling stone
heated solution 23 minute and Brown solution
chill in room temperature + 3 mL
NaOH 10% + 3 drops CuSO4 2%
Heated the solution Dark brown solution

G. PEMBAHASAN.

Percobaan ini bertujuan untuk membuktikan adanya ikatan peptida, dapat

memahami reaksi xanthoproteat dan uji biuret terhadap bermacam-macam
kandungan dari protein serta memahami kelarutan dan sifat amfoter dari asam
amino.
Prinsip dasar percobaan ini adalah mengidentifikasi asam amino dan
protein pada suatu larutan dengan pereaksi tertentu sedangkan prinsip kerjanya
adalah penimbangan, pencampuran, pengocokan, pemanasan, penguapan dan
penyaringan.
1. Kelarutan dan sifat amfoterik
Percobaan ini bertujuan untuk melihat kelarutan dan sifat amfoterik dari
asam amino. Sifat Amfoterik merupakan suatu keadaan dimana larutan dapat
bersifat asam maupun basa. Pada percobaan ini digunakan glisin, Asam L-
aspartat, dan L-tirosin.
a. Kristal glisin ditambahkan dengan aquades menghasilkan larutan bening.
Fungsi dari H2O yaitu sebagai pelarut untuk melarutkan kristal. Kemudian
diuji dengan menggunakan lakmus menghasilkan larutan bersifat asam.
Hal ini menunjukkan bahwa glisin bersifat polar hingga dapat larut dalam
air. Hal ini juga sesuai dengan teori yang menyatakan bahwa glisin bersifat
asam karena asam amino bersifat amfoterik yang mana dapat bersifat asam
 jika dalam larutan asam dan bersifat basa dalam larutan basa. Adapun
reaksi yang terjadi:
H H
-
H C COOH + H2O H C COO + H2O
+
NH 2 NH 3
( G lis in ) ( I o n Z w it t e r G lis in )

b. Percobaan untuk L-tirosin setelah ditambahkan dengan H2O Larutan

terdapat endapan putih, dan tidak larut dalam air dan bersifat netral. L-
tirosin tidak larut dalam air karena adanya gugus benzena yang terikat
pada L-tirosin, dimana sifat kepolaran air dan benzena berbeda. Air
bersifat polar sedangkan benzena bersifat nonpolar. Selain itu, perbedaan
densitas juga menyebabkan air dan benzena tidak dapat menyatu
sebagaimana yang kita ketahui bahwa densitas air adalah 1,00 g/mL
sedangkan benzena yaitu 0,88 g/mL (Material Safety Data Sheet).
Adapun reaksi yang terjadi :

- +
HO CH2 CHCOOH + H2 O HO CH2 CHCOO + H
+
NH 2 NH 3
( L - T ir o s in ) ( I o n z w it t e r L - T ir o s in )

c. Percobaan untuk asam L-aspartat setelah ditambahkan dengan H2O, asam

L-aspartat hanya larut sebagian dan terbentuk larutan keruh. Hal tersebut
memunjukan bahwa sikap kepolaran L-aspartat adalah rendah (non polar).
Setelah di uji dengan lakmus menghasilkan larutan yang bersifat asam. Hal
ini sesuai dengan teori yang menyatakan bahwa asam amino bersifat
amfoterik yang mana dapat bersifat asam jika dalam larutan asam dan
bersifat basa dalam larutan basa.
 H H
-
HOOC C COOH + H2O -
OOC C COO + H2O
+
NH 2 NH3
(A sa m L -a sp a rta t) ( I o n Z w it t e r a s a m
L -A sp a rta t)

d. Pengujian dengan L-tirosin ditambahkan air maka larutan berwarna putih

dan sedikit larut. kemudian ditambahkan dengan NaOH maka larutan tak
berwarna (larut), lakmus merah menjadi berwarna biru (basa), dimana
NaOH berfungsi untuk memberikan suasana basa dan sebagai penerima
proton sehingga larutan bersifat basa. Setelah itu larutan ditambahkan HCl
yang berfungsi untuk memberikan suasana asam dengan menyumbangkan
protonnya. Larutan tersebut menjadi putih dan diuji dengan kertas lakmus
biru, kertas lakmus biru menjadi lakmus merah (Asam). Adapun reaksi
yang terjadi, yaitu:

HO CH2 CHCOOH + H2 O + NaOH HO CH2 CHCOONa + 2H2 O

NH 2 NH 2

( L - T ir o s in ) ( A ir ) ( N a t r iu m ( N a t r iu m T ir o s in ) ( A ir )
H id r o k s id a )

HO CH2 CHCOONa + HCl HO CH2 CHCOOH + NaCl

NH2 NH 2
( N a t r iu m T ir o s in ) ( A s a m K lo r id a ) ( L - T ir o s in ) ( N a t r iu m k lo r id a )

e. Percobaan ini menggunakan kasein yang ditambahkan dengan air dan

NaOH terbentuk larutan koloid. Penambahan NaOH berfungsi untuk
memberikan suasana basa sehingga dapat melarutkan kasein. Dimana
kasein sukar larut dalam air bahkan tidak dapat larut karena banyaknya
rantai karbon yang terikat sehingga menyebabkan kelarutan kasein kecil.
Hal ini sudah sesuai dengan teori yang menyatakan bahwa R dari asam
amino yang terdiri dari banyak atom karbon atau aromatik sukar larut
dalam air (Tim Dosen Kimia Organik, 2017: 18). Adapun reaksi yang
 terjadi,yaitu:

O O O

HN CH C HN CH C HN CH C

CH 2 CH 2 CH 2 + H2O

OH OH OH n
K a s e in

2. Reaksi dengan Asam nitrit

Percobaan ini bertujuan untuk mendeteksi adanya gugus amin (-NH2) bebas
dalam asam amino yang ditandai dengan terbentuknya gas N2.
a. Kristal glisin yang direaksikan dengan HCl 10% menghasilkan larutan tak
berwarna, setelah didinginkan dan ditambahkan NaNO2 maka larutan tetap
tak berwarna dan terdapat banyak gelembung, dimana HCl berfungsi
memberi suasana asam yang akan bereaksi dengan NaNO 2 dan membentuk
HNO2 sedangkan NaNO2 berfungsi agar asam amino mampu bereaksi
dengan natrium nitrit menghasilkan gas N2 karena mengandung gugus
amina bebas. Tujuan dari pendinginan yaitu mempercepat proses
berlangsungnya reaksi.
b. Pada larutan HCl yang direaksikan NaNO 2 dan didinginkan menghasilkan
larutan yang tak berwarna dan terdapat sedikit gelembung. Fungsi dari
pendinginan yaitu mempercepat berlangsungnya reaksi dalam larutan karena
salah satu faktor laju reaksi adalah suhu. Gelembung yang dihasilkan hanya
sedikit karena tidak ada gugus amin yang bereaksi dengan HNO2 sehingga
tidak terbentuk gas N2.
c. Larutan kasein yang direaksikan dengan NaNO 2 menghasilkan larutan keruh
dan tidak terdapat gelembung. Tidak terbentuknya gelembung disebabkan
kasein tidak mempunyai gugus amin yang bebas.
3. Biuret Test
Pengujian ini bertujuan untuk membuktikan adanya ikatan peptida pada
protein yang ditandai dengan terbentuknya larutan berwarna ungu.
a. Pada percobaan ini urea dipanaskan menghasilkan gas NH 3 berbau tengik.
Pemanasan kemudian dilanjutkan sampai pembentukan gas berhenti dan
sisanya mulai padat. Pemanasan dilakukan bertujuan untuk mempercepat
terjadinya reaksi dan agar dapat membentuk gelembung gas. Padatan
dilarutkan dalam air kemudian disaring. Tujuan dari penyaringan adalah
agar dapat memperoleh larutan dengan partikel yang lebih kecil.
Kemudian ditambahkan larutan NaOH maka larutan berubah menjadi
bening. Penambahan NaOH berfungsi untuk mencegah endapan Cu(OH)2
yang mencegah ikatan protein, kemudian ditambahkan CuSO4, larutan
berubah menjadi ungu. Dimana CuSO4 yang berfungsi untuk mengetahui
ikatan adanya peptida pada asam amino yang ditandai dengan warna
larutan menjadi warna ungu. Larutan yang berwarna ungu menandakan
adanya ikatan peptida pada urea dimana apabila dipanaskan sehingga
melebihi titik leburnya maka urea tersebut akan berubah menjadi warna
ungu, ion tembaga (II) akan menghasilkan ion kompleks.
b. Sebagai pembanding, urea dilarutkan dengan H2O menghasilkan larutan
tak berwarna (urea larut) dan ditambahkan larutan NaOH untuk mencegah
adanya Cu(OH)2 yang memecah ikatan protein dan CuSO4 sebagai donor
Cu2+ sehingga menghasilkan warna biru. Hal ini menandakan bahwa tidak
terdapat ikatan peptida karena urea tidak dipanaskan sehingga tidak
terbentuk biuret. Reaksinya yaitu:

HN C NH 2 + NaOH + CuSO4

O
U re a

c. Kasein ditambahkan air menhasilkan larutan bening, kemudian

ditambahkan dengan larutan CuSO4 menghasilkan larutan berwarna ungu.
Hal tersebut menandakan bahwa pada kasein terdapat ikatan peptida.
4. Uji Xanthoproteat
Percobaan ini bertujuan untuk membuktikan adanya cincin aromatik dalam
protein yaitu cincin benzena. Pada percobaan ini kasein dilarutkan dengan asam
nitrat pekat menghasilkan larutan berwarna orange dan ada gumpalan kasein
kemudian dipanaskan dimana setelah pemanasan kasein telah larut. Fungsi
penambahan HNO3 pekat untuk melarutkan kasein dan juga akan bereaksi dengan
cincin benzena pada kasein membentuk nitro dengan proses nitrasi benzena.
Tujuan pemanasan yaitu untuk mempercepat berlangsungnya proses reaksi karena
salah satu faktor dari laju reaksi adalah suhu. Setelah dipanaskan, ditambahkan
dengan NaOH menghasilkan larutan berwarna kuning. Hal ini menandakan bahwa
adanya cincin aromatik pada kasein yang mengalami nitrasi pada saat
penambahan asam nitrat sehingga menghasilkan nitro yang berwarna kuning.
Fungsi penambahan NaOH adalah memberikan suasana basa dalam larutan dan
dapat bersifat katalis.
5. Hidrolisis Protein
Percobaan ini bertujuan untuk memutuskan ikatan peptida pada protein.
Pada percobaan ini kasein dilarutkan dalam HCl menghasilkan larutan berwarna
coklat keruh. Fungsi penambahan HCl adalah memberikan suasan asam dalam
larutan dan bersifat katalis untuk mempercepat reaksi. Dan tambahkan beberapa
baru didih fungsinya untuk peratakan panas. Setelah itu larutan dipanaskn.
Larutan dibagi dua agar dapat membandingkan hasil hidrolisis pada protein. Pada
larutan tersebut dimana Bagian pertama didinginkan dengan air es dan bagian
kedua didinginkan pada suhu kamar. Fungsi pendinginan untuk mempercepat
berlangsungnya reaksi dalam larutan karena salah satu faktor laju reaksi adalah
suhu. Larutan kedua ditambahkan dengan NaOH dan CuSO4. Fungsi penambahan
NaOH untuk memberikan suasana basa dan CuSO4 berfungsi untuk mengurai
protein menjadi asam-asam amino penyusunnya sehingga tidak ditemui lagi
ikatan peptidanya. Pada tabung pertama menghasilkan larutan berwarna coklat tua
sedangkan pada tabung berwarna coklat muda. Hal ini menandakan bahwa pada
kedua tabung proses hidrolisis ikatan peptidanya terputus. Hal ini sudah sesuai
dengan teori yang menyatakan bahwa hidrolisis protein akan menghasilkan asam-
asam amino (Tim Dosen Kimia Organik, 2017: 18).
H. CONCLUSIONS AND SUGGESTIONS
1. Conclusions
a. Amino acids are easily soluble in water if the C atom is short and will
be difficult to dissolve if it has a long C atom and is aromatic. Amino
acids are amphoteric and can react with both acids and bases.
b. Reaction with nitric acid this experiment aims to detect the presence of
a free amine group (-NH2) in the amino acid which is indicated by the
formation of N2 gas which is indicated by the appearance of bubbles.
c. Xanthoproteate reaction is a protein test to prove the presence of a
benzene ring in a protein. The xanthoproteate reaction was evidenced
by a yellow solution and the presence of lumps and a biuret test in the
presence of a purple solution.
d. Biuret test is a test to prove the presence of peptide bonds in proteins.
and the presence of lumps and a biuret test in the presence of a purple
solution.
e. Protein Hydrolysis, This experiment aims to break the peptide bonds in
proteins.
2. Suggestions
It is hoped that the practitioner will be careful and thorough in the
practicum in order to obtain results that are in accordance with the theory
and better master the experimental work procedures carried out.
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