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In situ entrapment of urease in cryogels of poly( N ‐isopropylacrylamide): An effective strategy for noncovalent immobilization of enzymes
Author(s) -
Petrov Petar,
Pavlova Severina,
Tsvetanov Christo B.,
Topalova Yana,
Dimkov Raycho
Publication year - 2011
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.34063
Subject(s) - urease , poly(n isopropylacrylamide) , lower critical solution temperature , urea , chemistry , chemical engineering , hydrolysis , membrane , polymer , polymer chemistry , swelling , immobilized enzyme , hydrogen peroxide , materials science , enzyme , organic chemistry , copolymer , biochemistry , engineering
Abstract Supermacroporous poly( N ‐isopropylacrylamide) (PNIPAAm) cryogels containing urease were prepared via UV irradiation technique and hydrogen peroxide as initiator. Specifically, due to the cryostructuration phenomenon urease molecules were embedded into the dense cryogel walls. Thus, although the enzyme is physically entrapped, the system exhibited remarkable resistance against leaking due to the dense polymer network formed in the cryogel walls. The immobilized urease can catalyze the hydrolysis of urea in a broad temperature range in both batch and flow regime. The interconnected macropores assist for unhindered diffusion of the substrate and reaction products through the gel, thus, paving the way for consecutive reuse at a constant activity, in contrast to the conventional PNIPAAm hydrogel. Due to the spongy‐like morphology PNIPAAm cryogels containing urease can be exploited as highly permeable membrane for direct removal of traces of urea from continuously flowing feed solutions. © 2011 Wiley Periodicals, Inc. J Appl Polym Sci, 2011