GELATIN AND COLLAGEN

M. Zakiyul Fikri
DEPARTEMEN KELAUTAN
FAKULTAS PERIKANAN DAN ILMU KELAUTAN
UNIVERSITAS AIRLANGGA

GELATIN
DEFINITION :
Protein derived from collagen via tropocollagen when
heated for an extended period; useful in gel formation.
(McWilliams, M. 1989)
Kristal polimer yang bersifat termoplastik dan viskoelastik.
(Phillips et al. 1989)
Stabilizing and gelling agent

Gelatin adalah derivat protein dari serat kolagen yang ada pada kulit,
tulang, dan tulang rawan. Susunan asam aminonya hampir mirip
dengan kolagen, dimana glisin sebagai asam amino utama dan
merupakan 2/3 dari seluruh asam amino yang akan menyusunnya,
1/3 asam amino yang tersisa diisi oleh prolin dan hidroksiprolin

Sifat gelatin tipe A dan tipe B

Standar mutu gelatin

Sumber: SNI 06-3735-1995

Persyaratan gelatin berdasarkan FAO

Sumber: JECFA (2003)

GELATIN STRUCTURE
CH2
CH2
CH2

CO-NH

CO

CHOH
CH2
CH

CH2

CH

NH

CO

CH-CO-NH CO CH-CO

R
GLISIN

CH2

PROLIN

CO

R
GLISIN

X HIDROKSIPROLIN

Struktur dasar kolagen (Gelse et al. 2003).

Molekul dasar pembentuk kolagen adalah tiga unit rantai

polipeptida yang saling berpilin membentuk struktur triple heliks
yang lebih dikenal dengan istilah tropokolagen

Kolagen triple heliks ini distabilkan terutama oleh ikatan hidrogen

baik ikatan intramolekul yang terjadi antara rantai-rantai molekul
tropokolagen maupun ikatan intermolekul antara molekul dalam
tropokolagen

COMPOSITION :

The origin of gelatin is the tropocollagen

strands of collagen, a protein in the
connective tissue of meat that undergoes
a change during heating. Three strands of
tropocollagen crosslink to form a fibrous
strand, and three of these strands then
crosslinks to form a molecule of the
connective tissue protein called collagen.

MANUFACTURING :
Commercially, gelatin is prepared by extraction
from bones and skins of meat animals. It can
be extracted by either acid or alkali treatment,
but alkali treatment is the method used most
commonly to obtain gelatin commercially.

This is a lengthy process requiring as long as

10 months of soaking in lime to obtain the
collagen stock and then several extraction with
hot water to obtain the gelatin from its parent
compounds.

PREPARATION
Skin/Bones

Extraction

Drying

Gelatin

The first extraction of gelatin from collagen stock yields a gelatin that
is fairly viscous, possesing a high gel strength. With subsequent
extractions, the viscosity and gel strength decline gradually.
Commercial gelatin are a blend of more than one extraction.
The final step in manufacturing gelatin is drying. The dried product
can be pulverized, granulated, flaked, or left in sheets. The form
available to the retail market is granulated gelatin.

PROPERTIES
Hydration
When gelatin is to be used in food preparation, the first step
Is to convert it form a firm, friable substance to one that is soft
and pliable
The elongated gelatin molecules have many polar groups exposed,
making it possible for water to be bound by hydrogen bonds at
many points along each molecule.
The swelling of gelatin resulting from the absorption of water is
influenced by the pH and the presence of salts.
Many gelatins, the pH at which hydration is at a maximum is around
pH 3.2 to 3.5 or 9.

PROPERTIES
Sol Formation
After hydration of gelatin in cold water, the swollen gelatin can be
dispersed readily in hot water or other hot liquid.
Apparently this ability to be dispersed as a sol is aided by the
physical dissociation of the gelatin molecules in their closely packed
dehydrated state.
The distancing that occurs between gelatin molecules weakens
intermolecular association and enables hot water to complete the
dissociation, allowing the long gelatin molecules to move freely as
the discontinuous phase in the sol.
The high temperature facilitates the breaking of week hydrogen
bonds that exist in the hydrated gelatin.
For gelatin to be an acceptable ingredient in any food product, the
individual molecules must be dispersed in very hot liquid.
When molecules adhere to each other rather than dispersing, their
fibrous and compact nature makes them quite rubbery and tenacious,
characteristics that definitely are undesirable in foods.

PROPERTIES
Enzymatic Hydrolisis
Papain

: Proteolytic enzyme in papaya capable of cleaving gelatin so

that it loses its gel-forming ability

Bromelin : Proteolytic enzyme in pineapple

Ficin

: Proteolytic enzyme in figs

Actinidin : Proteolytic enzyme in kiwi fruit

PROPERTIES
Gel Formation
Under appropriate conditions, a gelatin sol can convert to a gel as
the sol is cooled
The formation of gelatin gel is endothermic and occurs gradually as
the energy of the system dissipates. A surface film forms as some of
the gelatin molecules crosslink in a comparatively compact
configuration.

Thixotrophic : Capable of undergoing thixotrophy (the transition to a

sol from a gel on agitation)

PROSES PERUBAHAN KOLAGEN

MENJADI GELATIN

MELIPUTI :
1. PEMUTUSAN SEJUMLAH IKATAN PEPTIDA UNTUK
MEMPERPENDEK RANTAI
2. PEMUTUSAN/PENGACAUAN SEJUMLAH IKATAN SAMPING
ANTAR RANTAI
3. PERUBAHAN KONFIGURASI RANTAI

PROSES PEMBENTUKAN GEL PADA GELATIN

air

molekul gelatin
yang kompak

molekul
gelatin yang
panjang seperti
benang

air

SOL

GEL

(gelatin terdispersi dalam air)

(gelatin terdispersi dalam

jaringan gelatin)

COLLAGEN
Jaringan ikat terdiri dari serat protein kolagen dan
elastin yang mengandung polisakarida dan bermacammacam komponen organik dan anorganik

Komposisi :

Komponen asam amino yang paling banyak terkandung :

1/3 Glisin, 6-10 % Hidroksiprolin, 10-12 % Prolin
(komponen ini memberikan stabilitas termal pada kolagen)

RANGKAIAN

ASAM AMINO
Rantai polipeptida mengandung triple glisin dengan distribusi :

gly - x - x

Sangat polar

gly - x - l

gly - l - x

Non polar

gly - l - l
Keterangan :
l = residu asam amino (hidroksiprolin dan prolin)
x = residu asam amino lainnya

STRUKTUR KOLAGEN
Molekul dasar pembentuk kolagen disebut tropokolagen, yang mempunyai
struktur batang dengan berat molekul (BM) 300.000 dan didalamnya terdapat
tiga rantai polipeptida yang sama panjang membentuk struktur heliks.
Kolagen terdapat di jaringan dalam bentuk triple helix, yaitu molekul
tropokolagen yang dideretkan menurut susunan yang bergantian, seperempat
panjang tumpang tindih membentuk fibril yang bertumpuk-tumpuk sehingga
membentuk jaringan ikat.
Pembentukan struktur ini berlangsung dalam kondisi kandungan hidroksiprolin
dan hidroksisilin tinggi, kandunganasam amino dwi asam dan dwibasa tinggi,
serta triptofan dan sistin.
Susunan asam amino khusus tersebut mengakibatkan ikatan silang antar rantai
sehingga kolagen mudah menggembung dalam keadaan asam atau basa
(deMan 1997)

Pengelompokan tipe-tipe kolagen

Berdasarkan struktur dan
susunan supramolekul

PEPTIDE LINKAGE

PENGARUH PEMANASAN TERHADAP

STRUKTUR KOLAGEN
Pada saat suhu pemanasan mencapai 400C
Terjadi pemutusan ikatan hidrogen dan ikatan hidrofobik sehingga
berubah menjadi satu, dua, atau tiga molekul rantai acak.

Pada saat suhu pemanasan naik menjadi 600C

Ikatan kovalen pada kolagen terputus

Pemanasan serat kolagen dalam air hingga 600C-700C

Memperpendek serat sepertiga atau seperempat dari panjang asalnya

Jika suhu dinaikkan menjadi 800C

Kolagen berubah menjadi gelatin

PENGARUH PELARUT
ALKALI, ASAM DAN BASA
PELARUT ALKALI
Menyebabkan kolagen mengambang dan menyebar, dan kemudian
dikonversikan menjadi gelatin

PELARUT ASAM
Mampu mengubah serat kolagen triple heliks menjadi rantai tunggal

PELARUT BASA
Mampu menghasilkan rantai ganda

* Jumlah kolagen yang terhidrolisis dengan larutan asam lebih banyak daripada larutan
basa

PERBEDAAN HASIL HIDROLISIS

triple heliks kolagen

perendaman
asam

-heliks kolagen

perendaman
basa

-heliks kolagen

Hasil hidrolisis rantai triple heliks kolagen dengan

pelarut asam dan pelarut basa

APLIKASI
GELATIN DALAM INDUSTRI PANGAN dan NON PANGAN

INDUSTRI PRODUK OLAHAN DAGING

Contoh : SOSIS
- Sebagai penstabil emulsi
- Menghasilkan struktur gel yang kenyal

INDUSTRI FARMASI
- Bahan baku pembuatan kapsul
- Sebagai bahan tambahan

INDUSTRI FOTOGRAFI
Menstabilkan perak halida yang sensitif
terhadap sinar sebelum ditapiskan pada
lembaran film

APPLICATION
Food and Other Uses

Uses of Gelatin in Edible Products

Gelatin as a Jellying Agent
Gelatin as a Whipping Agent
Gelatin as a Stabilizer
Gelatin as an Emulsifier
Gelatin to Increase Viscosity
Gelatin as an Adhesive
Gelatin as a Binder

Gelatin as a Fining Agent

APPLICATION
Food and Other Uses

Uses of Collagen in Edible Products

Sausage Skins
Clarifying Reagent for Beer

APPLICATION
Food and Other Uses

Pharmaceutical and Medical Uses

Capsules
Tablets and Pastilles
Gelatin Dressing

Gelatin sponge
Surgical Powder
Suppositories
Medical Research
Plasma Expander

APPLICATION
Food and Other Uses

Microencapsulation

Sizing of Paper
Emulsification
Flocculation
Printing Application
Coated Abrasives

Adhesives Uses
Miscellaneous Uses

APPLICATION
Food and Other Uses

Printing Application
Carbon printing
Collotype
Silk screen printing
Photogravure
Wash of Process
Printers rollers

APPLICATION
Food and Other Uses

Adhesive Uses
Gummed paper tape
Carton and Box manufacturing
Furniture industry

Bookbinding
Modified adhesive

APPLICATION
Food and Other Uses

Miscellaneous Uses
Gelatin as a sizing agent
Manufacture of golf balls
Diffraction gratings and holographic plates
Cork composition
Paper gaskets
Bacterial culture media

Electrolytic metal refining

TERIMA KASIH
Selamat menempuh Ujian Akhir Semester (UAS)