In situ visualization and effect of glycerol in lipase-catalyzed ethanolysis of rapeseed oil |
| |
| Institution: | 1. Division of Aquaculture and Upgrading (DivAV), Portuguese Institute for the Sea and Atmosphere (IPMA, IP), Rua Alfredo Magalhães Ramalho, 6, 1495-006 Lisbon, Portugal;2. CIIMAR, Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Avenida General Norton de Matos, S/N, 4450-208 Matosinhos, Portugal;3. CIMA - Centro de Investigacións Mariñas, Pedras de Corón s/n. Apdo. 13, Vilanova de Arousa, 36620, Pontevedra, Spain;4. IGAFA - Instituto Galego de Formación en Acuicultura, Niño do Corvo s/n, 36626 Illa de Arousa, Pontevedra, Spain;5. ICBAS - Instituto de Ciências Biomédicas de Abel Salazar, University of Porto, Rua de Jorge Viterbo Ferreira, 228, 4050-313 Porto, Portugal |
| |
| Abstract: | Immobilized lipases can be used in biodiesel production to overcome many disadvantages of the conventional base-catalyzed process. However, the glycerol by-product poses a potential problem for the biocatalytic process as it is known to inhibit immobilized lipases, most likely by clogging of the catalyst particles. In this paper, this negative effect was further investigated and confirmed in ethanolysis of rapeseed oil. A dyeing method was developed for in situ visualization of glycerol in order to study its partitioning and accumulation during the ethanolysis reaction. The method was used to illustrate the interaction of glycerol with immobilized lipases and thus provided an aid for screening supports for lipase immobilization according to their interaction with glycerol. Glycerol was found to have great affinity for silica, less for polystyrene and no affinity for supports made from polymethylmethacrylate and polypropylene. It was also found that the immobilization of enzyme on the support influenced the adsorption of glycerol to the surface of the enzyme carrier. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
