Chitinases identified from Aeromonas schubertii by enzymomics techniques

Chitins, absent from vertebrates and plants, exist in arachnids, most of higher fungal cell walls, insect exoskeletons, the shells of crustaceans, and in parts of invertebrates. They are also present as an extracellular polymer of some bacteria. The formation rate and steady-state amount of chitin is about 10 gigatons every year. Most of the biological materials composed of chitin finally become biological solid waste and would be usually degraded by chitinases of microorganisms for nutrition purpose.

Chitinases are classified as endochitinases (EC 3.2.1.14), chitobiosidases (EC 3.2.1.30), and exochitinases (EC 3.2.1.52) on the catalytic mechanisms and products. They are distributed widely in organisms with chitin, such as bacteria, fungi, insects and crustaceans (CCC-7). In those, the enzymes are involved in development or growth. Usually, an organism poses more than one chitinase.

The suffix, omics, in life sciences represents the subject about whole knowledge, such as genomics, proteomics, metabolomics and so on. Proteomics is the investigation of proteome, the set of proteins encoded by the genome. That can be defined as the large-scale study of protein properties such as expression levels, post-translational modifications and interactions with other molecules to obtain a global view of cellular processes at the protein level. However, the proteins with quality changes are still ignored because there is no difference in 2DE.

Recently, a microorganism degrade chitin was isolated. The profiles of enzymes activities were screen by enzymomics techniques. The most potent chitinase was identified, cloned and expressed in the work.