Production, Properties, and Some New Applications of Chitin and Its Derivatives

Abstract

Chitin is a polysaccharide composed from N-acetyl-D-glucosamine units. It is the second most abundant biopolymer on Earth and found mainly in invertebrates, insects, marine diatoms, algae, fungi, and yeasts. Recent investigations confirm the suitability of chitin and its derivatives in chemistry, biotechnology, medicine, veterinary, dentistry, agriculture, food processing, environmental protection, and textile production. The development of technologies based on the utilization of chitin derivatives is caused by their polyelectrolite properties, the presence of reactive functional groups, gel-forming ability, high adsorption capacity, biodegradability and bacteriostatic, and fungistatic and antitumour influence. Resources of chitin for industrial processing are crustacean shells and fungal mycelia. Fungi contain also chitosan, the product of N-deacetylation of chitin. Traditionally, chitin is isolated from crustacean shells by demineralization with diluted acid and deproteinization in a hot base solution. Furthermore, chitin is converted to chitosan by deacetylation in concentrated NaOH solution. It causes changes in molecular weight and a degree of deacetylation of the product and degradation of nutritionally valuable proteins. Thus, enzymatic procedures for deproteinization of the shells or mold mycelia and for chitin deacetylation were investigated. These studies show that chitin is resistant to enzymatic deacetylation. However, chitin deacetylated partially by chemical treatment can be processed further by deacetylase. Efficiency of enzymatic deproteinization depends on the source of crustacean offal and the process conditions. Mild enzymatic treatment removes about 90% of the protein and carotenoids from shrimp-processing waste, and the carotenoprotein produced is useful for feed supplementation. In contrast, deproteinization of shrimp shells by Alcalase led to the isolation of chitin containing about 4.5% of protein impurities and recovery of protein hydrolysate.