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Chapter: Pharmacognosy and Phytochemistry : Enzymes and Protein Drugs

Gelatin is a protein derivative obtained by evaporating an aqueous extract made from bones, skins, and tendons of various domestic animals. Some important sources are: Ox, Bos taurus, and Sheep, Ovis aries belonging to family Bovidae






Gelfoam; puragel; gelatinum.


Biological Source


Gelatin is a protein derivative obtained by evaporating an aqueous extract made from bones, skins, and tendons of various domestic animals. Some important sources are: Ox, Bos taurus, and Sheep, Ovis aries belonging to family Bovidae




The process of manufacture of gelatin vary from factory to factory. However, the general outline of the process is given below.


Raw material


Bones, skins, and tendons of Bovideans is collected and subjected to liming operation.


Liming Process


The raw material is first subjected to the treatment known as ‘liming’. In this process, the skins and tendons are steeped for fifteen to twenty and sometimes for 40 days in a dilute milk of lime. During this, fleshy matter gets dis-solved, chondroproteins of connective tissues gets removed and fatty matter is saponified. The animal skin is further thoroughly washed in running water.




In case of bones, the material is properly ground and defatted in close iron cylinders by treatment with organic solvents such as benzene. The mineral and inorganic part of the bone is removed by treatment with hydrochloric acid.




The treated material from bones, skins and tendons is boiled with water in open pans with perforated false bottom. This process can also be carried out under reduced pressure. The clear liquid runs of again and again and is evaporated until it reaches to above 45 per cent gelatin content.




The concentrated gelatin extract is transferred to shallow metal trays or trays with glass bottom. It is allowed to set as a semisolid jelly.




The jelly is transferred to trays with a perforated wire netting bottom and passed through series of drying compartments of 30–60°C increasing each time with 10°C. About a month is taken for complete drying.




In case of darker colour, finished product is subjected to bleaching by sulphur dioxide. Bleaching affords a light coloured gelatin.




Gelatin occurs as a colourless or slightly yellow, transparent, brittle, practically odourless, tasteless sheet, flakes or course granular powder. In water it swells and absorbs 5–10 times its weight of water to form a gel in solutions below 35–40°C. It is insoluble in cold water and organic solvents, soluble in hot water, glycerol, acetic acid; and is amphoteric. In dry condition it is stable in air, but when moist or in solution, it is attacked by bacteria. The gelatinizing property of Gelatin is reduced by boiling for long time. The quality of gelatin is determined on the basis of its jelly strength (Bloom strength) with the help of a Bloom gelometer. Jelly strength is used in the preparation of suppositories and pessaries.


Commercially two types of gelatin, A and B, are avail-able. Type A has an isoelectric point between pH 7 and 9. It is incompatible with anionic compounds such as Acacia, Agar and Tragacanth. Type B has an isoelectric point between 4.7 and 5, and it is used with anionic mixtures. Gelatin is coloured with a certified colour for manufacturing capsules or for coating of tablets. It may contain various additives.


Chemical Constituents


Gelatin consists of the protein glutin which on hydrolysis gives a mixture of amino acids. The approximate amino-acid contents are: glycine (25.5%), alanine (8.7%), valine (2.5%), leucine (3.2%), isoleucine (1.4%), cystine and cysteine (0.1%), methionine (1.0%), tyrosine (0.5%), aspartic acid (6.6%), glutamic acid (11.4%), arginine (8.1%), lysine (4.1%), and histidine (0.8%). Nutritionally, gelatin is an incomplete protein lacking tryptophan. The gelatinizing compound is known as chondrin and the adhesive nature of gelatin is due to the presence of glutin.


Chemical Tests

1. Biuret reaction: To alkaline solution of a protein (2 ml), a dilute solution of copper sulphate is added. A red or violet colour is formed with peptides containing at least two peptide linkages. A dipeptide does not give this test.


2. Xanthoproteic reaction: Proteins usually form a yellow colour when warmed with concentrated nitric acid. This colour becomes orange when the solution is made alkaline.


3. Millon’s reaction: Millon’s reagent (mercuric nitrate in nitric acid containing a trace of nitrous acid) usually yields a white precipitate on addition to a protein solution which turns red on heating.


4. Ninhydrin test: To an aqueous solution of a protein an alcoholic solution of ninhydrin is added and then heated. Red to violet colour is formed.


5. On heating gelatin (1 g) with soda lime, smell of ammonia is produced.

6. A solution of gelatin (0.5 g) in water (10 ml) is precipitated to white buff coloured precipitate on addition of few drops of tannic acid (10%).


7. With picric acid gelatin forms yellow precipitate.



Gelatin is used to prepare pastilles, pastes, suppositories, capsules, pill-coatings, gelatin sponge; as suspending agent, tablet binder, coating agent, as stabilizer, thickener and texturizer in food; for manufacturing rubber substitutes, adhesives, cements, lithographic and printing inks, plastic compounds, artificial silk, photographic plates and films, light filters for mercury lamps, clarifying agent, in hectographic matters, sizing paper and textiles, for inhibiting crystallization in bacteriology, for preparing cultures and as a nutrient.


It forms glycerinated gelatin with glycerin which is used as vehicle and for manufacture of suppositories. Combined with zinc, it forms zinc gelatin which is employed as a topical protectant. As a nutrient, Gelatin is used as commercial food products and bacteriologic culture media.


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