Authors: Wazé Aimée Mireille Alloue Jacqueline Destain Thami El Medjoub Hakim Ghalfi Philomène Kabran Philippe Thonart
Publish Date: 2008/03/08
Volume: 150, Issue: 1, Pages: 51-63
Abstract
The purpose of this study was to immobilize lipase from Yarrowia lipolytica using three methods including inclusion adsorption and covalent bond to study enzyme leaching storage and catalytic properties Sodium alginate and chitosan were the polymers selected to immobilize lipase by inclusion The beads of each polymer were dried by freeze drying and fluidization The results show that chitosan was more adapted to the inclusion of lipase Even though freeze dried bead activity was low compared to that of fluidized beads The freezedrying process seems to produce suitable beads for storage at 4 and 20 °C The immobilization by adsorption was carried out on both celite and silica gel Maximum immobilization yield of 76 was obtained with celite followed by 43 in silica gel The enzyme adsorbed on the two supports exhibited greater stability at a certain temperature 50 °C and in no polar solvents Isooctane nheptane and nhexane In addition the lipase immobilized by covalent bond retained residual activity equitable to 70 It was demonstrated that the enzyme immobilized by covalent bond showed greater activity 80 after 5 months of storageThe authors thank the government of Ivory Coast for the financial support of this work via the scholarship We also wish to thank Prof Yves Poumay Mr Yves Houbion and Mr Renaud Vigneron of the Scanning Electron Microscopy Services at University of Namur Belgium for their valuable support and technical assistance
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