New Aspects of the Enzymatic Breakdown of Chitin: A Review

Abstract

This review focuses on the enzymatic breakdown of chitin, taking into account the latest scientific reports on the activity of lytic polysaccharide monooxygenase (LPMO). Chitin is a natural, abundant polysaccharide of great practical importance in the environment. However, the insolubility in water and the tightly packed crystalline structure of chitin pose a serious obstacle to enzymatic degradation. This substrate can be converted into soluble sugars by the action of glycosidic hydrolases (GH), also known as chitinases. LPMO could prove to be helpful in enzymatic processes that increase the rate of chitin depolymerisation by improving the availability of substrates for chitinases. The unique action of LPMO is based on the ability to catalyse the oxidative cleavage of glycosidic chains present in complex, resistant crystal networks of chitin, and this cleavage facilitates the subsequent action of glycolytic hydrolases.

Study of the binding of ΔFN3.1 fragments of the Bifidobacterium longum GT15 with TNFα and prevalence of domain-containing proteins in groups of bacteria of the human gut microbiota

“…Mutations in this motif alter the receptor's ability to bind cytokines [8] . In bacteria, FN3 domains are found in proteins with different enzymatic functions: cellulases [11,12] , hydrolases [1,13] , chitinases [14,15] , and proteases [16] . Presumably, FN3 domains play a structural, stabilizing role in ensuring the normal functioning of the enzyme [12] .…”