Chitin (C8H13O5N)n (pron.: /ˈkaɪtɨn/ KY-tin) is a long-chain polymer of a N-acetylglucosamine, a derivative of glucose, and is found in many places throughout the natural world. It is the main component of the cell walls of fungi, the exoskeletons of arthropods such as crustaceans (e.g., crabs, lobsters and shrimps) and insects, the radulas of mollusks, and the beaks and internal shells of cephalopods, including squid and octopuses. In terms of structure, chitin may be compared to the polysaccharide cellulose and, in terms of function, to the protein keratin. Chitin has also proven useful for several medical and industrial purposes.
The English word "chitin" comes from the French word chitine, which first appeared in 1821 and derived from the Greek word χιτον (chiton), meaning covering.
A similar word, "chiton", refers to a marine animal with a protective shell (also known as a "sea cradle").
The structure of chitin was solved by Albert Hofmann in 1929.
Chitin is a modified polysaccharide that contains nitrogen; it is synthesized from units of N-acetylglucosamine (to be precise, 2-(acetylamino)-2-deoxy-D-glucose). These units form covalent β-1,4 linkages (similar to the linkages between glucose units forming cellulose). Therefore, chitin may be described as cellulose with one hydroxyl group on each monomer replaced with an acetyl amine group. This allows for increased hydrogen bonding between adjacent polymers, giving the chitin-polymer matrix increased strength.
In its unmodified form, chitin is translucent, pliable, resilient, and quite tough. In arthropods, however, it is often modified, becoming embedded in sclerotin, a tanned proteinaceous matrix, which forms much of the exoskeleton. In its pure form, chitin is leathery, but in most invertebrates it occurs largely as a component of composite materials. Combined with calcium carbonate, as in the shells of Crustacea and molluscs, chitin produces a much stronger composite. On the one hand the composite is harder and stiffer than pure chitin, while on the other hand it is tougher and less brittle than the mineral substance alone. Another difference between pure and composite forms can be seen by comparing the flexible body wall between the segments of a caterpillar (mainly chitin) to the stiff, light elytron of a beetle (containing a large proportion of sclerotin).
Chitin was probably present in the exoskeletons of Cambrian arthropods such as trilobites. The oldest preserved chitin dates to the Oligocene, about 25 million years ago, comprising a scorpion encased in amber.
Most recent studies point out that chitin is a good inducer for defense mechanisms in plants. It has also been assessed as a fertilizer that can improve overall crop yields. The EPA regulates chitin for agricultural use within the USA. Chitosan is prepared from chitin by deacetylation.
Chitin is used in industry in many processes. Examples of the potential uses of chemically modified chitin in food processing include the formation edible films and as an additive to thicken and stabilize foods and pharmaceuticals. It also acts as a binder in dyes, fabrics, and adhesives. Industrial separation membranes and ion-exchange media can be made from chitin. Processes to size and strengthen paper employ chitin..
Chitin's properties as a flexible and strong material make it favorable as surgical thread. Its biodegradibility means it wears away with time as the wound heals. Moreover, chitin has some unusual properties that accelerate healing of wounds in humans.
Occupations associated with high environmental chitin levels, such as shellfish processors, are prone to high incidences of asthma. Recent studies have suggested that chitin may play a role in a possible pathway in human allergic disease. To be specific, mice treated with chitin develop an allergic response, characterized by a build-up of interleukin-4-expressing innate immune cells. In these treated mice, additional treatment with a chitinase enzyme abolishes the response.
Chitin may be employed for affinity purification of recombinant protein. A chitin binding domain is genetically fused to a protein of interest and then contacted to beads coated with chitin. The immobilized protein is purified and released from the beads by cleaving off the chitin binding domain.[clarification needed]
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