Masaaki Kawabe

Immobilization of Pseudomonas cepacia lipase onto electrospun polyacrylonitrile fibers through physical adsorption and application to transesterification in nonaqueous solvent

The lipase of Pseudomonas cepacia was immobilized onto electrospun polyacrylonitrile (PAN) fibers and used for the conversion of (S)-glycidol with vinyl n-butyrate to glycidyl n-butyrate in isooctane. The rate of reaction with the adsorbed lipase was 23-fold higher than the initial material. After 10 recyclings, the initial reaction rate was 80% of the original rate. This system of enzyme immobilization is therefore suitable for carrying out transesterification reactions in nonaqueous solvents.

Production of butyl-biodiesel using lipase physically-adsorbed onto electrospun polyacrylonitrile fibers.

Butyl-biodiesel production using electrospun polyacrylonitrile fibers with Pseudomonas cepacia lipase immobilized through physical adsorption was studied. About 80% conversion to butyl-biodiesel was achieved after 24h by suspending the catalyst at 2.4 mg/mL in a mixture of rapeseed oil and n-butanol at a molar ratio of 1:3, containing water at 8000 ppm at 40 degrees C. A further 24h of operation resulted in 94% conversion. The initial reaction rate detected for this process was 65-fold faster than those detected for Novozym 435 on a total catalyst mass basis. The immobilized lipase continued to work as a catalyst for 27 d, within a 15% reduction in conversion yield at the outlet of the reactor compared with the average value detected during the first 3d of operation in a continuous butyl-biodiesel production system.