Modern biorefineries provide a framework for the sustainable conversion of biomass to biofuels and biochemicals. In light of the recalcitrance of lignin in woody feedstocks, the native shrub eastern leatherwood is proposed as a model hypolignified species. Xylem tissue of this low-lignin plant contained syringyl-rich lignin that was more easily hydrolysed and did not appear to be localised in the middle lamellae. Also, leatherwood cellulose was less crystalline and the xylan was highly acetylated. While viable low-lignin plants will enable the sustainable utilisation of woody feedstocks, high-value bioproducts are needed to economise future biorefineries. The carbohydrate oxidoreductases galactose oxidase and glucooligosaccharide oxidase were studied for use in the oxidation and derivatisation of plant-derived polysaccharides for the production of such high-value bioproducts. The carbohydrate-binding module of galactose oxidase was necessary for recombinant protein production. Also, a mutant library of glucooligosaccharide oxidase variants was produced to generate enzymes with novel activity.

Modern biorefineries provide a framework for the sustainable conversion of biomass to biofuels and biochemicals. In light of the recalcitrance of lignin in woody feedstocks, the native shrub eastern leatherwood is proposed as a model hypolignified species. Xylem tissue of this low-lignin plant contained syringyl-rich lignin that was more easily hydrolysed and did not appear to be localised in the middle lamellae. Also, leatherwood cellulose was less crystalline and the xylan was highly acetylated. While viable low-lignin plants will enable the sustainable utilisation of woody feedstocks, high-value bioproducts are needed to economise future biorefineries. The carbohydrate oxidoreductases galactose oxidase and glucooligosaccharide oxidase were studied for use in the oxidation and derivatisation of plant-derived polysaccharides for the production of such high-value bioproducts. The carbohydrate-binding module of galactose oxidase was necessary for recombinant protein production. Also, a mutant library of glucooligosaccharide oxidase variants was produced to generate enzymes with novel activity.