In situ entrapment of urease in cryogels of poly(N‐isopropylacrylamide): An effective strategy for noncovalent immobilization of enzymes
In situ entrapment of urease in cryogels of poly(N‐isopropylacrylamide): An effective strategy for noncovalent immobilization of enzymes
复制标题
聚(N-异丙基丙烯酰胺)冷冻凝胶中脲酶的原位捕获:酶非共价固定的有效策略
DOI:
10.1002/app.34063
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发表时间:
2011
影响因子:
3
通讯作者:
R. Dimkov
中科院分区:
文献类型:
--
作者:
P. Petrov;S. Pavlova;C. Tsvetanov;Y. Topalova;R. Dimkov
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