Levoglucosan could be obtained by biomass pyrolysis and chemically transformed to high-added value compounds becoming a promising platform molecule.

Immobilization of enzymes is important to improve their stability and to facilitate their recyclability, aiming to make biocatalytic processes more efficient. One of the important aspects is the utilization of cheap, abundant, and environmentally friendly carriers for enzyme immobilization. Here we report the use of functionalized cellulose for lipase and transaminase immobilization. High immobilization efficiencies (up to 90%) could be achieved for the transaminase from Vibrio fluvialis. For immobilized lipase CAL-B as well as the transaminase, good conversions and recyclability could be demonstrated in kinetic resolutions to afford chiral alcohols or amines. Moreover, such application of the immobilized transaminase enabled very high conversions in a continuous-flow process in the asymmetric synthesis of (S)-phenylethylamine (80% conversion, >99% ee).

Among several value-added products from glycerol, glyceryl carbonate (GC) has gained prominence during the recent years because of its attractive physicochemical properties and the wide range of industrial applications. As a continuation of our efforts on GC production under environmentally benign conditions, in this work, we have applied a combination of two new biocatalysts containing lipases from porcine pancreas and Candida antarctica immobilized on epoxy resins for GC production via an integrated reaction between triacylglycerol and dimethyl carbonate under both batch and packed-bed reactors. Under continuous flow conditions, the 1:1 (w/w) combination of the home-made immobilized biocatalysts was able to lead to complete conversion of GC with >99% selectivity against 88% demonstrated by the commercial preparation Novozym 435. The new continuous flow biocatalytic system demonstrated a final productivity of 16 × 10^–2 g of GC/h/U of the biocatalyst.

Several value-added products can be produced from glycerol and among these products glycerol carbonate (GC) has received much attention in recent years because of its physical properties and wide application in the chemical, pharmaceutical and food industries. As a continuation of our efforts to produce GC under environmentally acceptable conditions, we proposed a consecutive approach where lipase B from Candida antarctica was immobilized on Accurel MP1000 (CalBAcc) under continuous-flow conditions followed by glycerol carbonate production by a cascade process of triacylglycerol hydrolysis, biodiesel synthesis and esterification of the remaining glycerol with dimethyl carbonate towards GC production. Results of the immobilization of lipase B from Candida antarctica on a continuous-flow protocol demonstrated that a short residence time of 25 minutes could lead to 83% of protein loading. Screening of glycerol carbonate production in a packed bed reactor revealed that CalBAcc and N435 showed the best results of conversion and selectivity, with more selectivity by CalBAcc, that could lead to quantitative yields and excellent selectivities of the desired glycerol carbonate at residence times of 176 minutes when working with soybean and palm oil. Comparatively, the results obtained with CalBAcc were better than the ones with Novozym 435 since no full conversion was observed.