Highly efficient immobilization of glycosylated enzymes into polyurethane foams.
Glycosylated enzymes, including aminoacylase from Aspergillus melleus, chloroperoxidase from Caldariomyces fumago, and phytase from Aspergillus ficuum, were covalently immobilized into polyurethane foams with very high enzyme loadings of up to 0.2 g protein per gram dry foam. The immobilization efficiency (retained activity) ranged from 100% at a low loading to 60% at high loadings. In contrast to many other immobilization methods no leaching of the enzyme from the support took place under the reaction conditions. In short, a universal method for the immobilization of enzymes from fungal sources was developed, affording a highly active, stable, and reusable biocatalyst.
Bakker
M
M
Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
van De Velde
F
F
van Rantwijk
F
F
Sheldon
R A
RA
D010832:6-Phytase / Q000737:chemistry; D000581:Amidohydrolases / Q000737:chemistry; D001230:Aspergillus / Q000201:enzymology; D019149:Bioreactors; D001709:Biotechnology; D002711:Chloride Peroxidase / Q000737:chemistry; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006031:Glycosylation; D003904:Mitosporic Fungi / Q000201:enzymology; D011140:Polyurethanes
D004800:Enzymes, Immobilized; D011140:Polyurethanes; C028279:polyurethane foam; D002711:Chloride Peroxidase; D010832:6-Phytase; D000581:Amidohydrolases; C019672:aminoacylase I