Phosphorylase hybrid structures with amylose

The glycogen phosphorolysis of phosphorylase can be reverted, which makes it possible to enzymatically polymerize amylose as well as hybrid structures with amylose as outlined in the following section. 

The strict primer dependence of the glycogen phosphorylases makes them ideal candidates for the synthesis of hybrid structures of amylose with non-natural materials... 

The strict primer dependence of the glycogen phosphorylases makes them ideal candidates for the synthesis of hybrid structures of amylose with non-natural materials (e.g., inorganic particles and surfaces, synthetic polymers). For this, a primer functionality (maltooligosaccharide) can be coupled to a synthetic structure and subsequently elongated by enzymatic polymerization resulting in amylose blocks. 

As shown above, hybrid structures bearing amylose blocks can be synthesized by covalent attachment of primer recognition units for phosphorylase and subsequent enzymatic grafting from polymerization. Following the same route we are currently synthesizing hybrid materials bearing (hyper)branched polysaccharide structures as shown in figure 6 with the described tandem reaction of two enzymes. 

Another tjqie of comb like amylose hybrids synthesized via enzymatic grafting with phosphorylase is based on polysiloxane backbones. To achieve these structures double bonds were incorporated to the reducing end of oligosaccharides which were then attached to poIy(dimethylsiloxane-co-methylsiloxane) copolymers via hydrosililation or to silane monomers which were subsequently polymerized to polysiloxanes . Various mono-, d>-, tri and oligosaccharides were attached to siloxane backbones and their solution properties were studied with viscosimetry and static and dynamic light... 

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