Gelatin is a protein rather than a polysaccharide. It is produced by acid (type A) or alkali (type B) treatment of collagen obtained from pig skin, cattle hides, and bones. While gelatin contains 18 different amino acids, about 95% of the structure is composed of 7. The amino acid sequence of most of the chain is a tripeptide repeating unit of (glycine)-(proline or hydroxyprolineMalanine, glutamic acid, aspartic acid, or arginine). Gelatin contains no tryptophan.

The important functional properties in food applications of gelatin (3) are gel strength, gelling temperature, setting rate, pH, and isoelectric pH. Typical values for some of these properties are as follows:

a net positive charge and will interact with negatively charged polymers such as agar, carrageenans, algins, low-methoxyl (LM) pectins, and gum arabic.

Although gelatin could be used in a variety of food products, its use is essentially limited to preparation of meltable-in-the-mouth water-dessert gels (gelatin desserts), meat products, and marshmallows and other confectioneries. It is also used to stabilize emulsions; as a stabilizer for ice cream and other dairy products; as a clarifying agent for wines, vinegar, and juices; and in bakery fillings and icings. It is not normally used as a thickener but is used to thicken low-fat spreads where the gel structure is broken down by processing and tempered by hydrophobic ingredients such as oils and emulsifiers.

Type Gel strength, g Bloom pH Isoelectric pH

The presence of ash, sulfur dioxide, and peroxides can affect product appearance, that is, can cause gel cloudiness and/or discoloration, but do not affect functional properties. The gelling temperature of gelatin solutions is related to concentration. Below pH 5, types A and B gelatins have

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