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 its 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-PGProline constrains bond angles proline 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; three intertwined helical strands Much more extended than alpha helix, with a rise per 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 protein about 2800 long and 14-15 in diameter It consists of three poly peptide chains wound around each other in a suprahetical fashion

The Different Polymorphic forms

type Chain Composition Distribution

[a1()]2, a2(I) Skin,bone,Tendons ,blood vessel,cornea [al()]3 blood vessel babys 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 converted from a reducible form to a more stable nonreducible form (The nature of the mature nonreducible cross-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 crosslinking than do fish that are well fed

Collagenases

Have a little activity against native collagen Difficult to dect (because it exhibits low activity) Seem to be of same importance in postmortem 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-togelatin transition During the transition, many noncovalent bonds are broken along with some covalent inter and intermolecular bonds and a few peptide bones If the collagen molecule was completely unstructured, then glue instead of gelatin is produced.

Processing

First Step The removal of noncollagenous components from 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 heating 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 collagens activity stronger, Keep the water from evaporating, Improve the exist environment of the skin cell, Accelerate the circle,irrigation the skin,delay the aging,cosmetology,remove the crinkle and so on.

Keep the Miosture

As the collagen molecule contain a lot of hydrophilic group.