Thermostable α-Glucan Phosphorylase-Catalyzed Enzymatic Copolymerization to Produce Partially 2-Deoxygenated Amyloses

α-Glucan phosphorylase catalyzes the enzymatic polymerization of α-d-glucose 1-phosphate (Glc-1-P) monomers from a maltooligosaccharide primer to produce α(1→4)-glucan—i.e., amylose. In this study, by exploiting the weak specificity for the substrate recognition of a thermostable α-glucan phosphorylase (from Aquifex aeolicus VF5), we investigated the enzymatic copolymerization of 2-deoxy-α-d-glucose 1-phosphate (dGlc-1-P), which was produced in situ from d-glucal, with Glc-1-P to obtain non-natural heteropolysaccharides composed of α(1→4)-linked dGlc/Glc units—i.e., partially 2-deoxygenated amylose. The reactions were carried out at different monomer feed ratios using a maltotriose primer at 40 °C for 24 h. The products were precipitated from the reaction medium, isolated by centrifugation, and subjected to 1H NMR spectroscopic and powder X-ray diffraction measurements to evaluate their chemical and crystalline structures, respectively. Owing to its amorphous nature, the partially 2-deoxygenated amylose with adapted unit ratios formed a film when subjected to a casting method.