COLLAGEN AND GELATIN

Chapter 14

Collagen
A major component of connective tissue. It contributes significantly to the toughness of meat product. Collagen is abundant in tendons, skins and bones. It comprises about 33% of the total proteins of mammals Part of collagen is soluble in netraul salt solutions, part is soluble in acids, but part of collagen remains insoluble.

Collagen

Glycine comprises 33% of amino acids and is distributed uniformely at every third position. The repetitive occurrence does not include first 14 amino acids from Nterminus and first 10 amino acids from C-terminus of collagen molecule. These peptides are known as telopeptides. Colllagen contains also hydroxyproline (up to 10%) and hydroxylysine. Hydroxyproline contribute to the stabilization of collagen. Collagen low in hydroxyproline denature at lower temperature (fish collagen)

Collagen
Collagenase is the only enzyme that can

hydrolyse native collagen. Clostridia produce this enzyme Noncollagenase proteases may only cleave the collagen telopeptide sites.

Collagen
Tropocollagen is a long cylindrical protein

fibre that consists of three polypeptide chains wound around each other in superhelical fashion.

Collagen - structure

Collagen structure
Polypetides in tropocollagen may be

crosslinked with covalent bonds. The number of crosslinks increases with animal age. Toughness of meat depends on the extent of crosslinks.

Collagen occurs in several polymorphic forms

Collagen type I - has two identical polypeptide chains. Found in skin, tendon and bones. Collagen type III - has three identical polypetide chains. Found in muscle. Collagen type IV - consist of polypetide chains of dissimilar size. Collagen type V - composition is not very clear

Collagen

Collagen can shrink to less than 33% of their original length at the temperature referred to as shrinkage temperature. This temperature is characteristic of species from which the collagen is derived. The shrinkage involves the collapse of tripple helical structure. The midpoint of collagen-to gelatin transition is defined as the melting temperature. Transition of collagen to gelatin involves breaking down both noncovalent bonds as well as some covalent bonds (Shiff bases and alsol condensation bonds).

Processing of collagen to gelatin involves:

Removal of non-collagenous material

by

acid or alkali Conversion of collagen to gelatin by heating in the presence of water Refining and Drying gelatin

Gelatin
Moisture

9-12% Ash 2% Gelatin lacks tryptophan and is deficient in sulfur containing amino acids

Gelatin may be used as:

Gelling agent Stabilizer Emulsifier Thickener Foaming agent Water binder Crystal growth modifier Glaze Adhesive

GELATINS
Gel Formation

Three Phases
Hydration
Cool Water 1 T Gel C H2O

Dispersion Gelation

Hot Water 100

Refrigeration

Stiffness of gelatin gel depends on:

concentration of gelatin acidity sugar physical interference

temperature
presence of enzymes

GELATINS
Factors Influencing Gel Formation

Concentration 1-2% Temperature Cool Avoid Freezing Sugar Delays Gel Weakens Structure Acid Weakens Structure Enzymes Bromelin Papain Actinidin Ficin Salts Strengthens Structure Added Solid Ingredients Weaken
Small Amount Finely Chopped Just before Gel Sets

GELATINS
Whipping

Whip or Sponge
Gel Combined w/ Beaten Egg Whites or Whipped Cream

Foam Increase 2-3 x Volume Dried Cool Dry Many Months

Too Long Lose Ability to Hydrate Serve Immediately

Storage

Prepared