Daniel Bartosik

Abstract Carbohydrate esterases modify polysaccharides by removing different ester moieties thereby affecting their physicochemical properties and their accessibility by glycoside hydrolases. We determined the full-length structures of two members (Fl8CE20_II and PpCE20_II) from the carbohydrate esterase family 20 (CE20) by X-ray crystallography that feature an ancillary domain, inserted into the catalytic SGNH-hydrolase domain.

CAZymes carbohydrate-active enzymes LTER long-term ecological research MAGs metagenome-assembled genomes PCoA principal coordinate analysis R2 Pearson correlation coefficient Just as other meta-omics technologies, microbial metaproteomics expands the application of proteomics from pure cultures and simple model systems to complex biological systems consisting of entire microbial communities and possibly host cells [1].

1 Introduction Modern biotechnological research has made the sustainable manufacturing of chemicals, pharmaceuticals, and other high-value products a major objective in response to growing environmental concerns and depleting petrochemical supplies. Exploiting renewable resources and developing enzyme-based processes as a sustainable route toward the extraction of valuable components are key elements of these efforts.