Chitin is one of the most common structure giving polysaccharides and can be naturally found in e.g. fungi and arthropods. It is used to produce the commercially interesting chitosan, which has increasing applications in industries like pharma, agriculture and food, textile and cosmetics. The degradation of chitin to chitosan is carried out by deacetylation, either using alkaline or in a more environmentally friendly manner via biocatalysts.
Among others, the lytic polysaccharide monooxygenases (LPMOs) are key enzymes in the degradation of crystalline polysaccharides like chitin by catalyzing oxidative cleavage of glycoside bonds. This reaction is only inefficiently performed by chitinases, as these enzymes mainly act on degrading amorphous chitin. LPMOs could perform as precursors for chitinases by oxidizing the crystalline surface of chitin and by that introducing new access points for chitinases. The efficiency of LPMOs is promoted by various carbohydrate-binding modules, however, structural and functional properties of these modules are unknown.
A team around Vincent G. H. Eijsink from the Norwegian University of Life Science together with scientists from the research department of EUCODIS revealed structural and functional variation between two chitin-binding domains and their significant effects on the catalytic performance of LPMOs. This research is paving the way towards a better understanding of LPMOs and their application in the industry to make crystalline chitin more accessible for green chitosan production.
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