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Covalent Enzyme Immobilization onto Photopolymerized Highly Porous Monoliths
Author(s) -
Pierre S. J.,
Thies J. C.,
Dureault A.,
Cameron N. R.,
van Hest J. C. M.,
Carette N.,
Michon T.,
Weberskirch R.
Publication year - 2006
Publication title -
advanced materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 10.707
H-Index - 527
eISSN - 1521-4095
pISSN - 0935-9648
DOI - 10.1002/adma.200600293
Subject(s) - covalent bond , candida antarctica , immobilized enzyme , polymerization , grafting , lipase , lysine , porosity , materials science , enzyme , chemical engineering , polymer chemistry , combinatorial chemistry , organic chemistry , polymer , chemistry , biochemistry , amino acid , engineering
Enzymes covalently immobilized on highly porous materials are demonstrated to have very high biocatalytic activity and good recyclability, exemplified by Candida antarctica Lipase B (CAL‐B). Polymerized high internal phase emulsions (PolyHIPEs, see figure) are developed for covalent grafting of proteins (enzymes) via the reaction of the protein surface lysine residues with active ester moieties in the monolithic material.