Collagen

Source
 Tendons
 Skin
 Bone
 Vascular system of animals
 The connection tissue sheaths surrounding
muscle
 Contribution of Collagen

The major fraction of connective tissue is

collagen
 This component is important because it

contributes significantly to toughness in

mammalian muscle
 Gelatin serves as the functional ingredient in

temperature
—Dependent Gel-type desserts
 Solubility

 Some of the collagen is soluble in neutral salt

solution
 Some in soluble in acid
 Some is insoluble
 Collagen
the secrets of it’s a.a.composition
 Nearly one residue out of three is Gly
 Proline content is unusually high
 Unusual amino acids found:
-4-hydroxyproline
-3-hydroxyproline
-5-hydroxylysine
-Pro and HyPro together make 30% of res
Collagen

 Regular primary structure -HP-P-G-P-P-

G-
proline
 Proline constrains bond angles
 Forms triple helix
 stabilized by H-bonds
glycine carbon
nitrogen
oxygen
 The collagen triple helix
A case of structure following composition
 The unusual amino acid composition of collagen is
unsuited for alpha helices or beta sheets
 But it is ideally suited for the collagen triple helix; thr
ee intertwined helical strands
 Much more extended than alpha helix, with a rise p
er residue of 2.9 Angstroms
 3.3residues per turn
 Long stretches of Gly-Pro-Pro/Hyp
 The Fabric of Collagen

 The collagen monomer is a long cylindrical pr

otein about 2800 Å long and 14-15 Å in diam
eter
 It consists of three poly peptide chains wound
around each other in a suprahetical fashion
The Different Polymorphic forms

胶原的主要类型 
type Chain Distribution
Composition
Ⅱ [a1(Ⅰ)]2, a2(I) Skin,bone,Tendons
,blood
vessel,cornea
Ⅲ [al(Ⅲ)]3 blood
vessel ， baby’s
skin
 Type (IV)
Like Type (III)
Contains Oxidizable cysteine residues
 Type (V)
Like Type (VI)
It is rich in hydroxyproline and hydroxylysine
content
But contains no cysteine
 Collagen Oxidations

 Protein to hydroxyproline

 Lysine to hydroxyproline

Are catalyzed by protine hydroxylase and lysine

hydroxylase respectively
 Collagen Cross-links

 As animals age ,collagen cross-links are conv

erted from a reducible form to a more stable
nonreducible form
(The nature of the “mature” nonreducible cros
s-link is not known)
 The number of cross-links in collagen also
increases with increasing age. This is why
meat older animals is older than that from
younger animals,even though muscles from
younger animals generally contain more
collagen.
 In fish, the situation is very different.
 The change of the Solubility

 As cross-linking of collagen increases it

becomes less soluble in a variety of solvents,
such as salt and acid solutions.
 The amount of insoluble collagen of cod
increases only slightly with age.
 Starring fish produce more collagen and
collagen with a greater degree of cross-
linking than do fish that are well fed
 Collagenases

 Have a little activity against native collagen

 Difficult to dect (because it exhibits low activit
y)
 Seem to be of same importance in postmorte
m tenderization
 Indiarubber man
This is because of the shortage of
Collagenases
 Conversion of collagen to Gelatin

 The shrinkage temperature

Collagen fibrils shrink to less than one-third
their original length at a critical temperatures
 This shrinkage involves a disassembly of
fibers and a collagen of the triple-helical
arrangement of polypeptide subunits in the
collagen molecule
 The melting temperature

 Definition:the midpoint of the collagen-to-gela

tin transition
 During the transition, many noncovalent bond
s are broken along with some covalent inter a
nd intermolecular bonds and a few peptide bo
nes
 If the collagen molecule was completely unst
ructured, then glue instead of gelatin is produ
ced.
 Processing

 First Step
The removal of noncollagenous components f
rom the stock
It can be done with acid or with aikali
 Acid hydrolysis is a milder treatment
Solubility↑
Produced: Type A gelatins
isoelectric points : pH 6-9
 Alkali hydrolysis results in deamidation
produced : Type B gelatins
Isoelectric points : pH 5
 Second Step
The conversion of collagen to gelatin by heati
ng in the presence of water
 Finally recovery of gelatin in the final form
 Gelatin used to make Jello, Gummi Bears
 Meat Tenderization

 Conditioning
 Calcium Treatment
 Treatment by Exogenous Proteases
 Electrical Stimulation
 Mechanical methods
 Conversion of collagen to gelatin
occurs during normal cooking of meat
 Cooking for a long time in liquid can achieve
the desires tenderness
 The tenderness and flakiness of cooked fish
are due to the relative ease with their
collagen is converted to gelatin

Tough cut of meat Pot roast

The Efficiency of Collagen Product
 Alimentation
√Offer the necessary nutrion,
√ Make the skin collagen’s activity stronger,
√ Keep the water from evaporating,
√ Improve the exist environment of the skin
cell,
√ Accelerate the circle,irrigation the skin,delay t
he aging,cosmetology,remove the crinkle and
so on.
 Keep the Miosture

 As the collagen molecule contain a lot of

hydrophilic group.