Synthesis of oligo (1→5)-α-L- arabinofuranosides related to the plant polysaccharide pectin

Mathilde Daugaard

Research output: Book/ReportPh.D. thesisResearch

319 Downloads (Pure)

Abstract

A strong fundamental understanding of plant biology is essential for meeting society’s growing demand for safe and nutritious food, dietary fibers, clothes, and renewable energy sources for an increasing global population. The plant cell wall is one of the main targets for biotechnological research, as it represents almost 50% of plant biomass.
A major constituent of the plant cell wall is different complex polysaccharides. The knowledge about their detailed structure and function on a molecular level is far from complete, and structural studies are complicated by the great complexity of the cell wall. The diversity of polysaccharides and the microheterogeneity in the cell wall make it extremely challenging to isolate well-defined compounds after partial degradation of plant material. Chemical synthesis, on the other hand, is capable of producing structurally diverse oligosaccharides of excellent purity, and in larger quantities.
The objective of the present study is to design and execute chemical syntheses of well-defined pectic oligosaccharides. These can serve as models for the more complex polysaccharide network found in the plant cell wall. The chemical synthesis of two branched structures of oligo (1→5)-α-L-arabinofuranosides that are prominent side chains in RG-I is presented. By employing a disaccharide donor, the number of glycosylation reactions was reduced significantly and late stage regioselective deprotection made it possible to introduce different sidechains in the oligosaccharides.
The work done during an external research stay at University of Copenhagen is also described. This includes the implementation of a covalent linker system as an alternative to bovine serum albumin (BSA) for oligosaccharides, as well as the development of a microarray-based transglycosylation assay capable of screening for novel glycosyl transferase/hydrolase activities.
Original languageEnglish
PublisherDTU Chemistry
Number of pages156
Publication statusPublished - 2016

Cite this