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research
Hydrophobic adsorption and covalent immobilization of Candida antarctica lipase B on mixed-function-grafted silica gel supports for continuous-flow biotransformations
Authors
Anderson
Arroyo
+40 more
Ballesteros
Banet
Bickerstaff
Blanco
Bornscheuer
Boros
Boros
Cao
Chen
Csajági
Dragoi
Faber
Galarneau
Garcia-Galan
Hanefeld
Hellner
Hudson
Jas
Kirchning
Kirk
Laszlo
Lee
Lee
Liese
Lozano
López-Serrano
Mateo
Noureddini
Noureddini
Orita
Popat
Poppe
Rodgers
Ruiz Toral
Sheldon
Sheldon
Sheldon
Tomin
Wang
Weiser
Publication date
1 January 2013
Publisher
'Elsevier BV'
Doi
Cite
Abstract
Adsorption onto solid supports has proven to be an easy and effective way to improve the mechanical and catalytic properties of lipases. Covalent binding of lipases onto the support surface enhances the active lifetime of the immobilized biocatalysts. Our study indicates that mesoporous silica gels grafted with various functions are ideal supports for both adsorptive and covalent binding for lipase B from Candida antarctica (CaLB). Adsorption of CaLB on phenyl-functionalized silica gels improved in particular its specific activity, whereas adsorption on aminoalkyl-modified silica gels enabling covalent binding with the proper reagents resulted in only moderate specific activity. In addition, adsorption on silica gels modified by mixtures of phenyl- and aminoalkyl silanes significantly increased the productivity of CaLB. Furthermore, CaLB adsorbed onto a phenyl/aminoalkyl-modified surface and then treated with glutardialdehyde (GDA) as cross-linking agent provided a biocatalyst of enhanced durability. Adsorbed and cross-linked CaLB was resistant to detergent washing that would otherwise physically deactivate adsorbed CaLB preparations. The catalytic properties of our best immobilized CaLB variants, including temperature-dependent behavior were compared between 0 and 70 C with those of two commercial CaLB biocatalysts in the continuous-flow kinetic resolutions of racemic 1-phenylethanol rac-1a and 1-phenylethanamine rac-1b. © 2013 Elsevier Ltd
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info:doi/10.1016%2Fj.procbio.2...
Last time updated on 01/04/2019
Repository of the Academy's Library
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oai:real.mtak.hu:7271
Last time updated on 12/12/2013