Molecular Recognition of Natural and Non-Natural Substrates by Cellodextrin Phosphorylase from Ruminiclostridium Thermocellum Investigated by NMR Spectroscopy.

ABSTRACT: β-1→4-Glucan polysaccharides like cellulose, derivatives and analogues, are attracting attention due to their unique physicochemical properties, as ideal candidates for many different applications in biotechnology. Access to these polysaccharides with a high level of purity at scale is still challenging, and eco-friendly alternatives by using enzymes in vitro are highly desirable. One prominent candidate enzyme is cellodextrin phosphorylase (CDP) from Ruminiclostridium thermocellum, which is able to yield cellulose oligomers from short cellodextrins and α-d-glucose 1-phosphate (Glc-1-P) as substrates. Remarkably, its broad specificity towards donors and acceptors allows the generation of highly diverse cellulose-based structures to produce novel materials. However, to fully exploit this CD

SUBMITTER: Gabrielli V 

PROVIDER: S-EPMC9293210 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature