Sustainable chemicals from lignocellulosic biomass canacceleratematerial transition. Heterogeneous catalysts provide a superior alternativeto homogeneous catalysts for xylose dehydration to furfural, a promisingplatform chemical. This work uses 3D open-cell aluminum foam structuresas catalyst support for the biphasic furfural synthesis from biorefineryhydrolysate (obtained via birch pretreatment). 3D open-cell aluminumfoams were coated with commercial TiO2. The foams weredip-coated in a solid slurry consisting of TiO2 dispersedin water and binders. Coatings were found to be reproducible and mechanicallystable. Catalytic activity testing of the TiO2 foams showed∼60–70% furfural selectivity at near-complete xyloseconversion in the range of 170–190 °C. The enhanced masstransport properties of foams minimized the formation of insolublehumin species in the aqueous phase. Employing sec-butylphenol (SBP) as the organic extractant enables long-term operationfor at least 36 h. This is due to the coextraction of furfural and5-hydroxymethylfurfural (obtained from glucose in the feed). Varyingfoam thickness while maintaining constant mass of washcoat showedabsence of both external and internal mass transfer limitations. Finally,performing xylose dehydration at 190 °C using TiO2-coated foams enabled a remarkably high furfural productivity of5.8 × 10–2 gfurfural gcat–1 min–1, over an order of magnitudegreater than the highest reported in the literature.

Homogeneous immunoassays that allow direct in-sampledetectionof biomarkers provide an attractive alternative to traditional heterogeneousimmunoassays that require multiple washing and incubation steps. Wepreviously reported the development of RAPPID, a bioluminescent sensorplatform that uses split luciferase complementation to enable sandwichimmunoassays directly in solution. Although RAPPID provides many benefitsover traditional heterogeneous immunoassays, it requires protein G-mediatedphotoconjugation of split luciferase fragments to the Fc part of IgGmonoclonal antibodies. Here, we report a new generation of RAPPIDsensors (RAPPID-M) that do not rely on photoconjugation of proteinG, but instead use a generic antibody-binding domain derived fromprotein M. The use of protein M substantially expands the applicationof RAPPID to include protein G-incompatible but analytically importantmouse IgG1 antibodies, as well as scFv and Fab antibody fragments.Moreover, binding of protein M is found to be essentially irreversible,abolishing the need for photo-cross-linking. RAPPID-M thus improvesupon the original RAPPID platform by the mix-and-measure-type assemblyof antibody-split-luciferase conjugates and its compatibility witha broader scope of antibody types without compromising and even improvingthe analytical performance.