Struktur dan Fungsi Protein

Materi Kuliah
Pokok
TIK Sub Pokok bahasan
Bahasan
Protein Mahasiswa mampu Struktur kimia asam
menjelaskan struktur amino dan protein
serta fungsi protein Sifat fisikokimia
asam amino dan
protein
Klasifikasi protein
Denaturasi protein
Sifat fungsional
protein
Fungsi Protein
 Protein
Definisi : Protein adalah 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
 Protein
Fungsi bagi tubuh:
Pembangun struktur sel
Pengatur : syaraf, hormon, enzime
Transporter : haemoglobin, albumnin
Pertahanan : Antibodi

1 g/kg BB/hari
 Protein Function
Enzymes Catalytic activity A B
Transport
Bind & carry ligand molecules (hemoglobins)
Proteins
Storage Proteins Ovalbumin, ferretin, casein
Contractile Can contract, change shape (actin & myosins)
Proteins make up elements of cytoskeleton & muscles
Provide support: collagen fibers of tendons,
Structural
elastin of ligaments, keratin of hair & feathers,
Proteins
fibroin of silk & spider webs
Defensive Provide protection: antibodies (IgG), fibrinogen,
Proteins thrombin, and snake venoms
Regulatory Regulate metabolic processes: includes
Proteins hormones, transcription factors & enhancers
 Protein Content in Foods
Animal origin Protein (%) Plant origin Protein (%)
Milk Rice, whole 7.5-9.0
Whole, dried 22-25 Rice, polished 5.2-7.6
Skimmed, dried 34-38 Wheat, flour 9.8-13.5
Beef Corn meal 7.0-9.4
Dried 81-90 Potato 10-13
Roasted 72 Soybean 33-42
Egg Peanut 25-28
Whole, dried 35 Tapioca 1.3
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 L-Arginine L-Asparagine L-Aspartic acid

(Ala / A) (Arg / R) (Asn / N) (Asp / D)

L-Cysteine L-Glutamic acid L-Glutamine Glycine

(Cys / C) (Glu / E) (Gln / Q) (Gly / G)

L-Histidine L-Isoleucine L-Leucine L-Lysine

(His / H) (Ile / I) (Leu / L) (Lys / K)
 Struktur dan Singkatan 20 Asam Amino

L-Methionine L-Phenylalanin L-Proline L-Serine

(Met / M) (Phe / F) (Pro / P) (Ser / S)

L-Threonine L-Tryptophan L-Tyrosine L-Valine

(Thr / T) (Trp / W) (Tyr / Y) (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 Amino pI Asam Amino pI
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 H

R C COO- R C COO- + H+
NH3+ NH2

H H

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

H H H
OH- OH-
R C COOH R C COO- R C COO-
H+ H+
NH3+ NH3+ NH2

pH ~ 1 pH ~ 6 pH ~ 11
Kurva Titrasi Asam Amino
R-CHCO2-

NH2

pK2
pH

pI R-CHCO2-

R-CHCO2H NH3+

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
Functional Disrupting
Bond Type
groups involved solvents
Electrostatic: Carboxyl Salt solutions
-COO-+NH3- Amino High or low pH
Hydrogen bond Hydroxyl, Amide, Urea solutions
-(C=O)NH HO- Phenol
Hydrophobic Long aliphatic Detergents,
bonds chain, aromatic organic solvents
Disulfide bonds Cystine Reducing agents,
-S-S- sulfite, marcapto-
ethanol
 Protein Structure
Linear sequence of AA's from N-terminal to
Primary C-terminal
sequence NCC-NCC-NCC-NCC-NCC-NCC-NCC-
NCC
Regular, recurring orientations of AA's in a
Secondary
peptide chain due to H-bonds = alpha helix
structure
& beta sheets
3D - conformational shape due to weak
Tertiary electrostatic interactions with other atoms
Shape of most proteins is GLOBULAR
2 or more different polypeptides or sub-
Quaternary units interacting to give a unique 3D spatial
relationship
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 Protein bound to carbohydrate
and hemagglutinin
Lipoprotein: chylomicron Conjugated Protein bound to lipid LDL and
VLDL
Metalloprotein: hemoglobin Conjugated Protein bound to metal ferritin
and myoglobin
Phosphoprotein: casein Conjugated Protein bound to phosphorus
Komponen Perubahan Yang mungkin Terjadi selama Proses Pengolahan
Bahan Pangan dan Penyimpanan Pangan

Denaturasi (karena panas) yang akan

Protein 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)

Pembekuan dapat menyebabkan protein

mengalami perubahan konformasi dan
kelarutannya
 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 alpha-helix and
beta sheets in a protein and uncoils it into a
random shape.
 Protein Denaturation
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.
 Protein Denaturation
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
Protein Denaturation
Factors Influencing Protein
Denaturation
Denaturation

Heat
Alcohol
Acid or Base
Heavy metals
Reducing Agents
 Protein Denaturation
Effect of Heat
Heat can be used to disrupt hydrogen bonds
and non-polar hydrophobic interactions. This
occurs because heat increases the kinetic
energy and causes the molecules to vibrate so
rapidly and violently that the bonds are
disrupted.
The proteins in eggs denature and coagulate
during cooking. Other foods are cooked to
denature the proteins to make it easier for
enzymes to digest them.
 Protein Denaturation
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.
 Protein Denaturation
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.
 Protein Denaturation
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.
 Protein Denaturation
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
 Denaturasi
Perubahan struktur sekunder, tersier dan kuartener protein
Perubahan konformasi protein
Struktur primer tetap protein tidak terfragmentasi
 Denaturasi

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 Systems
Functional Property Mode of Action Food System
Protein solvation, pH
Solubility Beverages
dependent
Water absorption H-bonding of HOH, Meats, sausages.
and binding entrapment of HOH Breads, cakes
Thickening, HOH
Viscosity Soups, gravies
binding
Meats, sausages,
Protein acts as
Cohesion-adhesion baked goods, pasta
adhesive material
products
Hydrophobic
bonding in gluten,
Elasticity Meats, bakery
disulfide links in
gels (deformable)
Typical Functional Properties Performed
by Proteins in Food Systems
Functional Property Mode of Action Food System
Protein matrix
Gelation formation and Meats, curds, cheese
setting
Formation and
Sausages, soup,
Emulsification stabilization of fat
cakes
emulsions
Meats, sausages,
Fat adsorption Binding of free fat
donuts
Adsorption, Simulated meats,
Flavor binding
entrapment, release bakery, etc
Forms stable film to Whipped toppings.
Foaming
entrap gas dessert
 Factors Influencing the Functional
Properties of Food Proteins
Intrinsic Environmental Process
Factors Treatments
Composition of Water Heating
proteins pH pH
Conformation Temperature Salts
of proteins Oxidizing/ Reducing/
Mono- or multi reducing agents oxidizing
component Lipids. Flavors, agents
Homogeneity sugars Drying
heterogeneity Physical
modification
Chemical
modification
 Functional Properties of Proteins Displayed in
Interactions with Different Food Constituents
Interaction With
Water Water and Proteins Lipids or Gases
Wet ability Viscosity inducing Emulsifying ability
Swelling Gelling Emulsification
Rehydration Fiber forming stabilization
Water holding Dough forming Foaming ability
Solubility Membrane forming 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 interrelationship
Protein

Fat H2O TEXTURAL PROPERTIES

BINDING
PROPERTIES Fat Sorption Energy H2 O
Binding
Protein and Protein and Texturized
Bound Fat Sorbed H2O Texturization Protein

H2O
Solubility H+, OH-,
M+, A- H2O
Coagulum

SURFACE PROPERTIES Energy Coagulation

Protein in
solution Gelation
Fat
Emulsification Air
Energy Foaming H+, OH-,
Energy
M+, A- Gel
Protein Lipid Protein Air
Emulsion Foams
 Characteristics Affected by Food Proteins
Sweetness Bitterness Color
Turbidity
Color Coagulation
Taste
Flavor Mouthfeel

Smoothness
Appea-
rance Gelation
Solubility
Swelling
Thickening
Visco-
elasticity
Water
holding Hydra-
tion
Wettability
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 water-holding 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
Amino Acids
Taste/Flavor
Gly, Ala, Thr, Pro,
Sweet taste
Ser, Glu
Phy, Tyr, Arg, Leu,
Bitter taste
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.
 What is enzyme?
Specialized protein molecules that
speed up chemical reactions in
living cells (biological catalysts).
Specific for particular substances
Composed of 200-1000 amino
acids residues covalently linked.
Molecular weight: 12.000 1
million
 Sumber Enzim
Plant
Kedelai: lipoksigenase
Animal
Sapi: renin
Microbial sources
Bakteri asam laktat: memproduksi enzim
proteolitik membantu degradasi protein
keju
 Some Properties of Enzymes

Small inorganic ion that helps catalyze

Cofactor reactions
Exp. Cu+2 ; Mg+2 ; Mn+2, etc
Small, organic, non-protein ligands (such as
NAD+, B-vitamins), which catalyze reaction
Coenzyme
most often by gaining/losing electron, transfers
group or break bonds.
Reaction
E + S <---> ES <---> E + P sucrase reaction
path
Portion of enzyme protein that attaches to the
Active site substrate by means of weak chemical bonds
(H-bonds, ionic bonds, hydrophobic forces, etc)
 How to name enzyme?
By adding suffix ase to the name of
enzyme substrate or reaction. For example:
Urease: acts on urea
Glucose oxidase oxidizes glucose to gluconic
acid
By adding suffix in to the name of enzyme
source. For example:
Papain is obtained from papaya plant
 International Commission of Enzyme
Develop a systematic nomenclature and classification
scheme for enzyme.
Trivial name, systematic name, enzyme commission (EU)
number, specific reaction.
For example: amylase
Trivial name: -amylase
Systematic name: -1,4-Glucan-4-glucanohydrolase
EC number: 3.2.1.1
Reaction: hydrolysis of -1,4-glucan links
Enzyme is divided into six classes based on types of
reactions they catalyze:
Oxidoreductase (1); Transferase (2); Hydrolase (3); Lyase
(4); Isomerase (5); Ligase (6)
 Enzim Dalam Pengolahan Pangan

Dua kelompok enzim yang banyak

digunakan dalam pengolahan pangan:
Oksidoreduktase
Hidrolase
Yang jarang digunakan dalam pengolahan
pangan:
Liase
Ligase
 Oxidoreduktase (1)
Enzim yang dapat mengkatalisis reaksi oksidasi atau
reduksi suatu bahan.
Yang utama:
Oksidase: mengkatalisis reaksi antara substrat dengan
molekul oksigen.
Katalase, peroksidase, tirosinase, asam askorbat oksidase,
lipoxidase (lipoxygenase)
Dehidrogenase: enzim yang aktif dalam pengambilan atom
hidrogen dari substrat.
Suksinat dehidrigenase: memecah asam glutamat menjadi asam
ketoglutarat dan NH3
Laktat dehidrogenase: memecah asam laktat menjadi asam piruvat.
 Transferase (2)
Enzim yang ikut serta dalam reaksi pemindahan
(transfer) suatu radikal atau gugus (AB + C A +
CB).
Yang utama:
Fosforilase: memecah ikatan glikosida -1,4 pati
dengan pertolongan ion fosfat membentuk -D-
glukosa-1-fosfat.
Transfosforilase: memindahkan gugus fosfat dari
suatu molekul ke molekul lainnya, misal
memindahkan gugus fosfat dari ATP kepada
heksosa menghasilkan heksosa-monofosfat dan
ADP.
 Transferase (2)
Transaminase: mengkatalisis reaksi antara asam
amino dan asam -keto menghasilkan asam
amino baru dan asam keto baru. Misal reaksi antara
asam glutamat dan asam oksaloasetat
menghasilkan asam -ketoglutarat dan asam
aspartat.
Transmetilase: mengkatalisis pemindahan gugus
metil dari suatu mole-kul ke molekul lainnya. Contoh:
memindahkan gugus metil dari metionin kepada
asam guanidoasetat membentuk homosistein dan
kreatin.
Transasetilase: membentuk molekul bergugus
asetil.
 Hidrolase (3)
Mengkatalisis reaksi hidrolisis suatu substrat atau
pemecahan substrat dengan pertolongan molekul
air.
Yang utama:
Lipase: menghidrolisis ikatan ester pada lemak alami
menjadi gliserol dan asam lemak.
Glikosidase: menghidrolisis ikatan glikosida
Aminopeptidase (tripsin): menghidrolisis ikatan peptida.
Urease: menghidrolisis urea menjadi amonia dan CO2.
 Liase (4)
Enzim yang aktif dalam pemecahan ikatan
C-C dan ikatan C-O dengan tidak
menggunakan molekul air.
Yang utama:
Dekarboksilase: memecah ikatan C-C
Karbonat anhidrase: memecah ikatan C-O
 Isomerase (5)
Enzim yang mengkatalisis reaksi perubahan
konfigurasi molekul dengan cara pengaturan
kembali atom-atom dalam molekul substrat,
sehingga dihasilkan molekul baru yang merupakan
isomer dari substrat, misal merubah aldosa menjadi
ketosa.
Yang utama:
Fosfoheksosa isomerase: mengubah glukosa 6-P
(glukosa 6-fosfat) menjadi fruktosa 6-P
Fosfomanosa isomerase: merubah glukosa 6-P
menjadi manosa 6-P
 Ligase (6)
Mengkatalisis pembentukan ikatan-ikatan
tertentu, misalnya pembentukan ikatan C-
O, C-C dan C-S dalam biosintesis ko-
enzim A serta pembentukan ikatan C-N
dalam sintesis glutamin.
 Nomor Kode Enzim (EC)
Terdiri dari 4 digit:
Digit 1: Nomor urut dari salah satu 6
pembagian umum.
Digit 2: Subklas, substrat, atau jenis reaksi
Digit 3: Subklas, jenis reaksi yang lebih detail
lagi, biasanya memerlukan NAD dan ko-
enzim
Digit 4: nomor seri dalam subklas tersebut.
 Pedoman Klasifikasi Enzim
Oksidoreduktase
1.1. Bekerja pada gugus -CHOH
1.2. Bekerja pada gugus keton atau aldehida
1.3. Bekerja pada gugus -CH-CH-
1.4. Bekerja pada gugus CH-NH2
1.5. Bekerja pada gugus C-NH-
1.11. Bekerja pada gugus H2O2
 Pedoman Klasifikasi Enzim
Tranferase
2.1. Pemindahan (transfer) gugus satu carbon seperti
metil atau karboksil
2.2. Pemindahan gugus aldehida dan keton
2.3. Pemindahan gugus asil
2.4. Pemindahan gugus glikosil
2.5. Pemindahan gugus alkil
2.6. Pemindahan gugus nitrogen
2.7. Pemindahan gugus yang mengandung fosfor
2.8. Pemindahan gugus yang mengandung sulfur
 Pedoman Klasifikasi Enzim
Hidrolase
3.1. Bekerja pada ikatan ester
3.2. Bekerja pada senyawa glikosil
3.3. Bekerja pada ikatan ester-tio
3.4. Bekerja pada ikatan peptida
3.5. Bekerja pada ikatan C-N yang bukan peptida
3.6. Bekerja pada ikatan asam anhidrida
3.7. Bekerja pada ikatan C-C
3.8. Bekerja pada ikatan halida
 Pedoman Klasifikasi Enzim
Liase
4.1. Bekerja pada C=C-
4.2. Bekerja pada C=O
4.3. Bekerja pada C=N-
4.4. Bekerja pada C=S
4.5. Bekerja pada C-halida
 Pedoman Klasifikasi Enzim
Isomerase
5.1. Rasemase dan epimerase
5.2. Cis-trans isomerase
5.3. Oksidoreduktase intramolekul
5.4. Transferase intramolekul
5.5. Liase intramolekul
 Pedoman Klasifikasi Enzim
Ligase
6.1. Pembentukan ikatan C-O
6.2. Pembentukan ikatan C-S
6.3. Pembentukan ikatan C-N
6.4. Pembentukan ikatan C-C
 Nomenklatur enzim yang penting dalam
pengolahan pangan
No. EC Nama sistematiknya Nama trivial
1. Oksido-
reduktase
1.1.3.4. -D-glukosa: O2 Glukosa oksidase
oksidoreduktase
1.10.3.1 -difenol: 02 Katekol oksidase
oksidoreduktase
1.11.1.6 H2O2: H2O2 Katalase
oksidoreduktase
1.11.1.7 Donor: H2O2 Lipoksigenase/lipoksidase
oksidoreduktase
No. EC Nama sistematiknya Nama trivial
2. Transferase
2.1.1.5. -1,6-glucan; D-fruktosa 2 Dekstran sukrase
glukosil transferase
2.4.1.19 -1,4-glukan-4gliosil Enzim B. macerans
transferase
3. Hidrolase
3.1.1.1. Karbolik ester hidrolase Karboksil esterase
3.1.1.3. Gliserol ester hidrolase Lipase
3.1.1.11 Pektin pektil hidrolase Pektin esterase
3.2.1.1. -1,4-glukan glukanohidrolase -amilase
3.2.1.2. -1,4-glukan maltohidrolase -amilase
4. Isomerase
5.3.1.9. D-glukosa-6-fosfat ketol Glukosa isomerase
isomerase
 Faktor yang mempengaruhi
aktivitas enzim
Suhu
Mula-mula dengan meningkat suhu, aktifitas enzim meningkat.
Tetapi, pada suhu tertentu, enzim mengalami inaktivasi.
Pada suhu rendah, laju inaktivasi enzim sangat lambat
pH
Aktivitas maksimum: 4.5-8.0 (tergantung jenis enzim)
Pada kisaran pH di luar kisaran tersebut, umumnya enzim
mengalami inaktivasi.
Aktivitas air
Pada aw yang rendah, enzim tidak aktif.
Pada aw tinggi, enzim aktif
Garam
Kadar elektrolit yang tinggi umumnya mempengaruhi kelarutan
protein mempengaruhi aktifitas enzim.
 Pengaruh Suhu
Pada suhu rendah,
100 aktivitas enzim
lambat.
80
Keaktifan (%)

Aktivitas enzim
optimum: 45-55oC
60
Pada suhu tinggi, laju
40 inaktivasi enzim cepat
sekali, sehingga
20 reaksi enzimatik
praktis berhenti sama
10 20 30 40 50 60 70 sekali
Suhu (oC)
 Pengaruh pH
Enzim memiliki pH optimum
pH optimum
yang khas, yaitu pH yang
menyebabkan aktivitasnya
Laju reaksi

maksimal. pH optimum: 4.5-8.0.

Pada pH rendah aktivitas enzim
rendah. Pada pH yang lebih
tinggi aktivitas enzim menurun.

Contoh:
3 4 5 6 7 8 9 10 11 12 13
Terjadinya browning oleh enzim
Suhu (oC) fenolase dapat dihambat dengan
menurunkan pH larutan sampai pH
3.0, sebab pH optimal fenolase 6.5
pH optimum beberapa enzim
Pepsin : 1.5
Tripsin : 7,7
Katalase : 7.6
Arginase : 9,7
Fumarase : 7,8
Ribonuklease : 7,8
 Enzymatic reaction vs aw
At low Aw (<0.2), freely mobile water is not
available to carry out the reaction, and so
enzymatic reactions tend to be surpressed
in the lower regions of the sorption isotherm.
At high Aw, free water is available for the
enzymatic reaction.
For example: lipoxygenase starts to be
active after dry soybean (MC=14%) is
soaked in water off-flavor
 Rate of Enzymatic Reaction in Food as a
Function of Water Activity
Relative Reaction Rate Zone I Zone I Zone I

Moisture
content
isotherm

cti vity
a
n zyme
E

0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0

Water Activity
 Pengaruh Konsentrasi Substrat terhadap
kecepatan reaksi enzimatik

Pada konsentrasi substrat yang amat rendah,

kecepatan reaksi pun amat rendah.
Kecepatan reaksi akan meningkat dengan
meningkatnya konsentrasi substrat.
Pada titik tertentu, peningkatkan konsentrasi
substrat tidak dapat meningkatkan kecepatan
reaksi (enzim menjadi jenuh oleh substratnya
dan tidak dapat berfungsi lebih cepat).
Pada saat kecepatan reaksi tidak berubah lagi
disebut mencapai kecepatan Maksimum (Vmax)
 Pengaruh Konsentrasi Substrat Terhadap
Kecepatan Reaksi Enzimatik
Persamaan Michaelis-
Menten

Vmax Vmax [S]

Kecepatan reaksi

V=
KM + [S]

Dimana:
Vmax
V = kecepatan reaksi pada
konsentrasi substrat [S]
Vmax = kecepatan maksimum
KM = tetapan Michaelis-Menten
Konsentrasi Substrat, M enzim bagi substrat tertentu
 Persamaan Michaelis-Menten

KM
Sudut =
VMax
1
V
1 KM 1 1
= +
V VMax [S] VMax

1
VMax
1
1 [S]
KM