Protein

ITP 210
Kimia Pangan
MATERI KULIAH
Pokok
Bahasan
Protein
The
TIK
Sub Pokok
bahasan
Mahasiswa mampu Struktur kimia

asam amino dan
menjelaskan
protein
struktur serta
fungsi asam amino Sifat fisikokimia
asam amino dan
dan protein,
protein
termasuk enzim
Klasifikasi
protein
Denaturasi
protein
Sifat fungsional
protein
Enzim (tatanama
dan spesifisitas
First Food Technology Undergraduate Program Outside of North America
Approved by the Institute of Food
enzim)
PROTEIN
Makromolekul
(polipeptida) yang
tersusun dari asam amino yang
dihubungkan satu sama lain
dengan ikatan peptida.
Sumber:
Nabati
(kedelai, kacang-kacangan, dsb)

Hewani (daging, ikan, unggas, dsb)
Merupakan
molekul yang besar,

mengandung lebih dari 100 residu
asam amino.
Jenis: globular, fibrous, conjugated
The First Food Technology Undergraduate Program Outside of North America Approved by the Institute of Food
PROTEIN
Fungsi bagi
tubuh:
Pengatur
Pembangun
Aktivitas biologis
(hormon, enzim dll)
1 g/kg BB/hari
Protein Function
Enzymes
Catalytic activity A B
Transport
Proteins
Bind & carry ligand molecules

(hemoglobins)
Storage
Proteins
Ovalbumin, ferretin, casein
Contractile
Proteins
Can contract, change shape (actin &

myosins) make up elements of
cytoskeleton & muscles
Structural
Proteins
Provide support: collagen fibers of

tendons, elastin of ligaments, keratin of
hair & feathers, fibroin of silk & spider
webs
Defensive
Proteins
Provide protection:antibodies (IgG),

fibrinogen, thrombin,andsnake venoms
Regulate metabolic processes: includes

Regulatory
PROTEIN CONTENT IN FOODS

Animal origin
Protein
(%)
Milk
Plant
origin
Rice, whole
7.5-9.0
5.2-7.6
Whole, dried
22-25
Rice,
polished
Skimmed, dried
34-38
Wheat, flour
Beef
Dried
Roasted
Corn meal
81-90
72
Egg
Protein
(%)
9.8-13.5
7.0-9.4
Potato
10-13
Soybean
33-42
Peanut
25-28
1.3
Whole, dried
35
Tapioca
Whole, dried,
defatted
77
Chickpea
22-28
ASAM AMINO
Senyawa organik yang mengandung 2 gugus

fungsional:
Amin
(-NH2): Bersifat basa
Karboksil
(-COOH): Bersifat asam
Kedua gugus fungsional tersebut terikat pada

karbon (-karbon)
-C bersifat asimetrik (kecuali glisin): bersifat optik

aktif
Struktur dapat dinyatakan sebagai struktur ion

dipolar.
Bersifat amfoterik: dapat berperilaku sebagai asam

atau basa.
ASAM AMINO
Terdapat
20 jenis asam amino, yang

berbeda satu sama lain pada gugus R
yang terikat pada -karbon
Gugus R dapat bersifat gugus alifatik
non-polar, gugus alifatik polar, gugus
aromatik, dan bermuatan
positif/negatif.
Asam amino yang paling sederhana:
glisin (gugus R adalah H)
-C bersifat
asimetrik
(mengingat gugus
yang berbeda,
yaitu COOH,
-NH2, H dan R
Kecuali pada
Glisin, R-nya
adalah H
Struktur Ion Dipolar
KELOMPOK ASAM AMINO

BERDASARKAN SIFAT
KEPOLARAN
Non-polar, R gugus alifatik
Gugus
R tersusun dari gugus hidrokarbon yang

bersifat hidrofobik.
Glisin, alanin, valin, leusin, metionin, isoleusin
R gugus aromatik
Gugus R tersusun dari struktur cincin aromatik atau
sulfur
Fenilalanin, tirosin, triptofan
Polar, gugus R tidak bermuatan
Gugus R mengandung gugus hidroksil atau gugus
amino
Bersifat hidrofilik (dapat membentuk ikatan
hidrogen)
Serin, treonin, sistein, prolin, asparagin, glutamin
KELOMPOK ASAM AMINO

BERDASARKAN SIFAT
KEPOLARAN
R bermuatan positif
Gugus R mempunyai gugus amide yang dapat
membentuk ion positif pada pH di bawah 7.0
Lisin, arginin, histidin
R bermuatan negatif
Gugus R mempunyai gugus COOH yang dapat
membentuk ion negatif pada pH di atas 7.0
Asam aspartat, Asam glutamat
Struktur dan Singkatan 20 Asam Amino
L-Alanine
(Ala/A)
L-Arginine
(Arg/R)
LAsparagine
(Asn/N)
L-Aspartic
acid (Asp/D)
L-Cysteine
(Cys/C)
L-Glutamic
acid (Glu/E)
L-Glutamine
(Gln/Q)
Glycine
(Gly/G)
L-Histidine
(His/H)
L-Isoleucine
(Ile/I)
L-Leucine
(Leu/L)
L-Lysine
(Lys/K)
Struktur dan Singkatan 20 Asam Amino
LMethionine
(Met/M)
L-Phenylalanin
(Phe/F)
L-Proline
(Pro/P)
L-Serine
(Ser/S)
L-Threonine
(Thr/T)
L-Tryptophan
(Trp/W)
L-Tyrosine
(Tyr/Y)
L-Valine
(Val/V)
SIFAT IONISASI ASAM AMINO

Di
dalam larutan, asam amino terionisasi dan

dapat bersifat sebagai asam atau basa
(bersifat amfoter).
Dalam keadaan dipolar (zwitterion), dimana
gugus amin dan karboksil berionisasi, asam
amino memiliki kelarutan yang minimal.
Titik isoelektrik: pH pada saat molekul asam
amino tidak bermuatan
pK: pH pada saat gugus amino dan karboksil
50% terionisasi dan 50% tidak terionisasi.
TITIK ISOELEKTRIK ASAM

AMINO
Asam
pI
Asam
Amino
pI
Amino
Gly
6.0
Phe
5.5
Ala
6.0
Tyr
5.7
Val
6.0
Trp
5.9
Leu
6.0
Asp
3.0
Ile
6.0
Glu
3.2
Ser
5.7
Asn
5.4
Thr
5.6
Lys
9.7
Cys
5.0
Arg
10.8
Met
5.7
Gln
5.7
Pro
6.3
His
7.6
ELECTRICAL CHARGES
Some
individual amino acid residues in a

protein have the potential to be charged
electrically in different ways, depending on
the pH of the medium in which the protein is
found.
The individual protein molecules are said to
be amphoteric, because they have the
potential to function as either acid or a base,
depending on the pH.
Isoelectric point: when the number of
positive and negative charges are equal.
Protein has minimum solubility at the
isoelectric point.
Ionisasi Asam Amino

H
R
H
COO-
NH3+
+ H+
NH2
H
R
COO-
H
COO- + H+
NH3+
COOH
NH3+
(Zwitterion)
Ionisasi glisin pada berbagai nilai pH;

Contoh
H
R
H
COOH
NH3+
pH ~ 1
OHH+
H
COO-
NH3+
pH ~ 6
OHH+
COO-
NH2
pH ~
11
KURVA TITRASI ASAM AMINO

R-CHCO2NH2
pH
pK2
pI
R-CHCO2H
R-CHCO2NH3+
NH3+
pK1
Ekuivalen basa (OH-)

POLIMERISASI
Jenis
polimerisasi:
Dipeptida: 2 asam amino berikatan
Oligopeptida:
Polipeptida:
Protein:
Dihubungkan satu sama lain dengan
ikatan peptida
IKATAN PEPTIDA
Ikatan
peptida merupakan ikatan kovalen yang

menghubungkan antara gugus amin (-NH2) pada
AA1 dengan gugus karboksil (-COOH) pada AA2
Pada saat terbentuk ikatan peptida, 1 molekul
air dibebaskan (polimerisasi kondensasi)
Ikatan peptida lebih pendek dan lebih kuat
daripada ikatan C-C, tetapi lebih lemah
dibanding C=C.
Ikatan peptida tidak dapat berotasi secara bebas
Ikatan peptida
Pembentukan Ikatan Peptida Untuk

membentuk struktur
Protein/peptida
Reaksi Pembentukan
Peptida
Struktur Peptida hasil

polimerisasi
BONDS BETWEEN PROTEIN

CHAIN
Bond Type
Functional
groups
involved
Disrupting
solvents
Electrostatic:
-COO-+NH3-
Carboxyl
Amino
Salt solutions
High or low pH
Hydrogen bond
-(C=O)NH HO-
Hydroxyl,
Amide, Phenol
Urea solutions
Hydrophobic
bonds
Long aliphatic
chain, aromatic
Detergents,
organic solvents
Disulfide bonds
-S-S-
Cystine
Reducing
agents, sulfite,
marcaptoethanol
Protein Structure
Primary
sequence
Linear sequence of AA's from Nterminal to C-terminal

NCC-NCC-NCC-NCC-NCC-NCC-NCCNCC
Secondary
structure
Regular, recurring orientations of AA's

in a peptide chain due to H-bonds=
alpha helix & beta sheets
Tertiary
3D - conformational shape due

toweak electrostatic interactions
with other atoms
Shape of most proteins is
GLOBULAR
Quaternary
2 or more different polypeptides or

sub-units interacting to give a unique
Protein Structure
Struktur Protein
Struktur primer (ikatan
peptida)
Struktur Protein
Struktur Primer
Struktur Protein
Struktur sekunder (ikatan hidrogen)
-heliks protein
-sheet protein
sutera
Struktur Protein
Struktur tersier (disebabkan adanya
ikatan hidrogen, ikatan garam, interaksi
hidrofobik, dan ikatan disulfida)
Struktur Protein
Struktur kuartener (agregat beberapa unit
protein/ terdiri dari beberapa rantai
polipeptida)
Struktur Kuartener
TYPES OF PROTEIN
Globular
protein: native proteins that are

rather spherical in the configuration of their
tertiary structure. Exp. Albumin (egg),
globulin (meat, legume), histone (glandular
tissue), protamines (fish sperm cells)
Fibrous protein: Insoluble, elongated
protein molecules. Exp. Collagen, elastin (in
meats, poultry)
Conjugated protein: proteins combined
with some other type of compound, such as a
carbohydrate or lipid. Exp: mucoproteins
(glycoproteins), lipoprotein, metalloprotein,
nucleoprotein, phosphoprotein
EXAMPLE OF FOOD PROTEIN IN STRUCTURES

AND SHAPES
Food Proteins
Protein Structure Protein shape
Egg albumin
Globular
Spherical
Meat and legume globulins
Globular Spherical
Collagen
Fibrous
Elongated
Elastin
Fibrous
Elongated
Glycoprotein: ovomuvoid Conjugated

carbohydrate
Protein bound to
and hemagglutinin
Lipoprotein: chylomicron
and
Protein bound to lipid LDL

VLDL
Conjugated
Metalloprotein: hemoglobin
bound to metal ferritin
Conjugated
and myoglobin
Phosphoprotein: casein
Protein bound to phosphorus
Conjugated
Protein
Komponen
Bahan
Pangan
Protei
n
Perubahan Yang mungkin Terjadi selama Proses

Pengolahan dan Penyimpanan Pangan
Denaturasi (karena panas) yang akan

menyebabkan perubahan kelarutan,
sehingga mempengaruhi tekstur pada
bahan pangan
Penyimpangan flavor yang disebabkan
karena oksidasi (dikatalisis oleh
cahaya)
Degradasi enzimatik yang akan
menyebabkan perubahan pada tekstur dan
flavor (bisa menyebabkan terbentuknya
flavor pahit)
The
Pembekuan dapat menyebabkan protein

mengalami perubahan konformasi dan
First Food Technology Undergraduate Program Outside of North America Approved by the Institute of Food
PROTEIN DENATURATION
Denaturation
of proteins involves the

disruption and possible destruction of both
the secondary and tertiary structures.
Since denaturation reactions are not
strong enough to break the peptide bonds,
the primary structure (sequence of amino
acids) remains the same after a
denaturation process.
Denaturation disrupts the normal alphahelix and beta sheets in a protein and
uncoils it into a random shape.
Denaturation
occurs because the bonding

interactions responsible for the secondary
structure (hydrogen bonds to amides) and
tertiary structure are disrupted.
In tertiary structure there are four types of
bonding interactions between "side chains"
including: hydrogen bonding, salt bridges,
disulfide bonds, and non-polar hydrophobic
interactions, which may be disrupted.
Therefore, a variety of reagents and
conditions can cause denaturation.
The most common observation in the
denaturation process is the precipitation or
coagulation of the protein.
Unfolding
of protein structure (due to H

bonds breaking) without disrupting protein
covalent bonds.
Functional properties of protein will change
during denaturation (e.g. enzyme function
will be stopped; solubility in water will
decrease).
Example:
Thermal processing denatures the meat
protein actin, myosin and myoglobin.
Cooking egg denatures egg white
proteins including ovalbumin
FACTORS INFLUENCING
Denaturation
Heat
Alcohol
Acid or Base
Heavy metals
Reducing Agents
Effect
of Alcohol
Hydrogen bonding occurs between amide
groups in the secondary protein structure.
Hydrogen bonding between "side chains"
occurs in tertiary protein structure in a variety
of amino acid combinations. All of these are
disrupted by the addition of another alcohol.
Alcohol denatures proteins by disrupting the
side chain intramolecular hydrogen bonding.
New hydrogen bonds are formed instead
between the new alcohol molecule and the
protein side chains.
Effect
of Acids and Bases

Salt bridges result from the
neutralization of an acid and amine
on side chains.
The final interaction is ionic between
the positive ammonium group and
the negative acid group.
Any combination of the various
acidic or amine amino acid side
chains will have this effect.
Effect
of Acids and Bases

Acids and bases disrupt salt bridges
held together by ionic charges. A type
of double replacement reaction occurs
where the positive and negative ions in
the salt change partners with the
positive and negative ions in the new
acid or base added.
This reaction occurs in the digestive
system, when the acidic gastric juices
cause the curdling (coagulating) of
milk.
Effect
of Acids and Bases

The denaturation reaction on the
salt bridge by the addition of an acid
results in a further straightening
effect on the protein chain
Denaturas
Perubahan struktur sekunder, tersier dan kuartener pro

Perubahan konformasi protein
Struktur primer tetap protein tidak terfragmentasi
Denaturas
Flour Process Bread
FUNCTIONAL PROPERTIES
OF PROTEIN
Characteristics
that govern the

behavior of proteins in foods during
processing, storage, and preparation
as they affect food quality and
acceptance.
FISIKO-KIMIA PROTEIN
Hidrasi (daya ikat air/water holding

capacity) dan pembentuk viskositas
Kelarutan (penting untuk proses ekstraksi)
Pengental
Pembentuk gel (penting untuk produk
olahan daging dan ikan)
Pembentuk tekstur
Koagulasi panas dan pembentuk film
(seperti pada kembang tahu)
Texturized protein (pembentukan struktur
serat seperti daging pada produk
ekstrusi)
FISIKO-KIMIA
PROTEIN
Pengemulsi
Pembentuk busa (busa protein putih telur
melembutkan dan mengembangkan produk
cake)
Pembentuk adonan (protein gluten yang
bersifat viskoelastis pada adonan roti dan
mie)
Bersama-sama dengan gula pereduksi
membentuk warna dan aroma melalui
reaksi Maillard
TYPICAL FUNCTIONAL PROPERTIES

PERFORMED BY PROTEINS IN
FOOD
FunctionalSYSTEMS
Property
Solubility
Mode of Action
Food System
Protein solvation,
Beverages
pH dependent
H-bonding of
Water absorption
Meats, sausages.
HOH, entrapment
and binding
Breads, cakes
of HOH
Viscosity
Thickening, HOH
binding
Soups, gravies
Cohesionadhesion
Protein acts as
adhesive
material
Meats, sausages,
baked goods,
pasta products
Hydrophobic
bonding in
Elasticity
gluten, disulfide
Meats, bakery
links
inOutside
gelsof North America Approved by the Institute of Food
The First Food Technology Undergraduate
Program
TYPICAL FUNCTIONAL PROPERTIES

PERFORMED BY PROTEINS IN
FOOD SYSTEMS
Functional
Property
Mode of Action
Food System
Gelation
Protein matrix
formation and
setting
Meats, curds,
cheese
Emulsification
Formation and
stabilization of
fat emulsions
Sausages, soup,
cakes
Fat adsorption
Binding of free
fat
Meats, sausages,
donuts
Flavor binding
Adsorption,
entrapment,
release
Simulated meats,
bakery, etc
Forms stable film Whipped

to entrap gas
toppings. dessert
First Food Technology Undergraduate Program Outside of North America Approved by the Institute of Food
Foaming
The
FACTORS INFLUENCING THE

FUNCTIONAL PROPERTIES OF FOOD
PROTEINS
Intrinsic
Composition
of proteins
Conformation
of proteins
Mono- or multi
component
Homogeneity
heterogeneity
Environmental
Factors
Water
pH
Temperature
Oxidizing/
reducing agents
Lipids. Flavors,
sugars
Process
Treatments
Heating
pH
Salts
Reducing/
oxidizing
agents
Drying
Physical
modification
Chemical
modification
FUNCTIONAL PROPERTIES OF PROTEINS

DISPLAYED IN INTERACTIONS WITH
DIFFERENT FOOD
CONSTITUENTS
Interaction With
Water
Wet ability
Swelling
Rehydration
Water holding
Solubility
Water and Proteins

Viscosity inducing
Gelling
Fiber forming
Dough forming
Membrane forming
Lipids or Gases
Emulsifying ability
Emulsification
stabilization
Foaming ability
Foam stabilization
Influence to food materials:

Appearance, color, juiceness, mouth feel, texture
Cutting, mincing, mixing, formation of dough, fibers,
foils, bubbles, shaping, and transporting
ASPECTS OF PROTEIN
FUNCTIONALITY AND ITS
Protei
INTERRELATIONSHIP
n
Fat
BINDING
PROPERTIES
Fat
Binding
Protein
and
Bound
Fat
SURFACE PROPERTIES
Emulsificati
on
H2 O
Fat
Sorptio
Protein n
and
Sorbed
H2 O H2 O
Solubilit
y
Protein Lipid
Emulsion
Texturizatio
n
H+,
OH-,
M+, A-
Protein
in
Air
solution
Energ Foamin
y
g
TEXTURAL
PROPERTIES
H2 O
Energ
Energ
y
Protein
Air Foams
H2 O
Energ
y
H+,
OH-,
M+, A-
Texturiz
ed
Protein
Coagulu
m
Coagulati
on
Gelatio
n
Gel
CHARACTERISTICS AFFECTED BY FOOD

PROTEINS Bitterness
Sweetness
Color
Color
Coagulatio
n
Mouthfeel
Taste
Flavor
Solubility
Appearance
Swelling
Water
holding
Wettabilit
y
Turbidity
Smoothnes
s
Gelation
Thickenin
Viscoelasticity g
Hydration
Food
Characteristics
affected by
Proteins
EMULSIFICATION
Since
protein molecules contain

both hydrolytic and hydrophobic
characteristics, proteins can
stabilize emulsions by acting at
the oil-water interface.
This functional property is
important in the formation of
many common food products,
such as salad dressings, sauces,
frankfurters, and sausages.
Foods, such as meat tissue, milk,
eggs, and soy contain proteins
that can be isolated as
emulsifiers.
PROTEIN GELATION
Proteins
can form a well-ordered gel

matrix by balancing protein-protein and
protein-solvent interactions in food
products.
These
gel matrices can hold water, fat,

and other food ingredients to produce
various food products, including bread
dough, communited meat products,
gelatin desserts, tofu, and yoghurt.
Gelation Mechanism of
Protein
WATER HOLDING CAPACITY

The
ability of a protein molecule to bind

water has to do with the presence of
hydrophylic and charged groups in its
structure. This property is called waterholding capacity of protein
Example: meat retains water during
application of external forces such as
cutting, heating, grinding, and pressing.
Affected by: pH, salt, and temperature.
WATER HOLDING CAPACITY
When the negative and positive charges on a protein equal to

each other, protein : protein interactions are at maximum.
When the protein is not electrically neutral, these interactions

lessen, allowing for greater water: protein associations.
By increasing salt concentration, more Na+ and Cl- ions are

available to bind the charged groups on protein fiber
molecules. This reduces the protein fiber interactions with
each other in favor of increase protein fiber : water
associations.
As temperature increases to 80oC, water binding increases in

proteins that form thermally induced gels, because gelations
traps water inside a three-dimensional gel network in addition
to creating gel surface binding of water molecules.
PROTEIN FUNCTIONALITY:
FAT BINDING PROPERTIES
Hydrophobic proteins effectively lower surface

tension and bind many lipophilic materials, such
as lipids, emulsifiers, and flavor materials.
The capacity of protein to bind fat is important
in the production of meat extenders and
replacers, in which the absorption of fat by
proteins enhances flavor retention and
improves mouthfeel.
Fat is absorbed through physical entrapment.
Fat absorption can be increased if the protein is
modified chemically to increase its bulk density.
CONTRIBUTION OF
AMINO ACIDS TO TASTE
AND FLAVOR
Contribution to
Taste/Flavor
Amino Acids
Sweet taste
Gly, Ala, Thr,

Pro, Ser, Glu
Bitter taste
Phy, Tyr, Arg,

Leu, Val, Met, His
Umami and Sour

Glu, Asp
taste
Cheese and miso (soy sauce) are examples of
fermented foods whose flavor is largely caused
by their amino acid composition.
PROTEIN HYDROLYSIS
Protein molecules may undergo hydrolysis

to form shorter chains.
The reaction usually is the result of
enzymatic action by peptidases, but
sometimes collagen is cleaved by acid
hydrolysis.
The result if cleavage of the peptide bond
and uptake of a molecule of water
The shorter chains resulting from hydrolysis
show increased solubility and decreased
ability to thicken food products.
Degradasi enzimatik
Meningkatnya kandungan peptida dan asam
amino pada tempe (dikehendaki)
Meningkatnya kandungan peptida pada keju
karena pertumbuhan mikroba yang tidak
dikehendaki pada saat pemeraman,
menyebabkan keju berasa pahit.

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ITP 210

Mahasiswa mampu Struktur kimia

(kedelai, kacang-kacangan, dsb)

molekul yang besar,

Bind & carry ligand molecules

Ovalbumin, ferretin, casein

Can contract, change shape (actin &

Provide support: collagen fibers of

Provide protection:antibodies (IgG),

Regulate metabolic processes: includes

PROTEIN CONTENT IN FOODS

Senyawa organik yang mengandung 2 gugus

(-NH2): Bersifat basa

(-COOH): Bersifat asam

Kedua gugus fungsional tersebut terikat pada

-C bersifat asimetrik (kecuali glisin): bersifat optik

Struktur dapat dinyatakan sebagai struktur ion

Bersifat amfoterik: dapat berperilaku sebagai asam

20 jenis asam amino, yang

Struktur Ion Dipolar

KELOMPOK ASAM AMINO

R tersusun dari gugus hidrokarbon yang

KELOMPOK ASAM AMINO

Struktur dan Singkatan 20 Asam Amino

Struktur dan Singkatan 20 Asam Amino

SIFAT IONISASI ASAM AMINO

dalam larutan, asam amino terionisasi dan

TITIK ISOELEKTRIK ASAM

individual amino acid residues in a

Ionisasi Asam Amino

Ionisasi glisin pada berbagai nilai pH;

KURVA TITRASI ASAM AMINO

Ekuivalen basa (OH-)

peptida merupakan ikatan kovalen yang

Pembentukan Ikatan Peptida Untuk

Struktur Peptida hasil

BONDS BETWEEN PROTEIN

Linear sequence of AA's from Nterminal to C-terminal

Regular, recurring orientations of AA's

3D - conformational shape due

2 or more different polypeptides or

protein: native proteins that are

EXAMPLE OF FOOD PROTEIN IN STRUCTURES

Protein Structure Protein shape

Meat and legume globulins

Glycoprotein: ovomuvoid Conjugated

Protein bound to lipid LDL

Protein bound to phosphorus

Perubahan Yang mungkin Terjadi selama Proses

Denaturasi (karena panas) yang akan

Pembekuan dapat menyebabkan protein

of proteins involves the

occurs because the bonding

of protein structure (due to H

of Acids and Bases

of Acids and Bases

of Acids and Bases

Perubahan struktur sekunder, tersier dan kuartener pro

Flour Process Bread

that govern the

Hidrasi (daya ikat air/water holding

TYPICAL FUNCTIONAL PROPERTIES

TYPICAL FUNCTIONAL PROPERTIES

Forms stable film Whipped