β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: a comparative experimental and modelling study of the galactooligosaccharides production.

• Type: Article in International Conference Proceedings Book
• Date: 2008

Authors

Neri, David (Author) Other; Balcão, Victor (Author) Other; Costa, Rafael (Author) Other; Ferreira, Eugénio (Author) Other; Torres, Duarte (Author) FCNAUP; Rodrigues, Lígia (Author) Other; Carvalho Jr., Luiz (Author) Other; Teixeira, José (Author) Other

Conference proceedings International

Title: Proceedings of the 10th International Chemical and Biological Engineering Conference

Pages: 1036-1041

10th International Chemical and Biological Engineering Conference, CHEMPOR 2008

Braga, Portugal, 4 a 6 de Setembro

Scientific classification

FOS: Medical and Health sciences > Other medical sciences

CORDIS: Technological sciences > Technology > Production technology > Food technology ; Technological sciences > Technology > Biotecnology > Food biotechnology ; Natural sciences > Biological sciences > Biological engineering

Other information

Abstract (EN): β-Galactosidase from Aspergillus oryzae is an enzyme with a wide industrial application, mostly in the hydrolysis of lactose and, more recently, in the synthesis of oligosaccharides. Several advantages are associated with the application of immobilized enzymes on magnetic supports. In this work, β-galactosidase was covalently immobilised onto a Polysiloxane-Polyvinyl Alcohol Magnetic Composite (mPOS-PVA), Magnetic Polysiloxane with Polyaniline (mPOS-PANI), Magnetized Dacron (DACRON) and Magnetite with Polyaniline (MAG-PANI) using glutaraldehyde as activating agent being the synthesis of GOS evaluated and compared at different temperatures (30, 40, 50 and 60 oC) and various initial lactose concentration (50, 100, 200, 300, 400 and 500 g/L). The kinetic parameters obtained by fitting the experimental data were compared in order to determine the effect of the immobilization process with different supports on the synthesis of oligosaccharides. These results clearly demonstrate that all supports may be used for β-galactosidase immobilization as, besides improving the enzyme hydrolytic and GOS synthesis properties, its separation from the obtained reaction products is easy to accomplish

Language: Portuguese

Type (Professor's evaluation): Scientific