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Bicontinuous Nanoporous Frameworks: Caged Longevity for Enzymes
Author(s) -
Bae JaeSung,
Jeon Eunkyung,
Moon SuYoung,
Oh Wangsuk,
Han SunYoung,
Lee Jeong Hun,
Yang Sung Yun,
Kim DongMyung,
Park JiWoong
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201605609
Subject(s) - nanoporous , covalent bond , enzyme , chemical engineering , trapping , nanotechnology , immobilized enzyme , chemistry , materials science , catalysis , enzyme catalysis , organic chemistry , biology , ecology , engineering
The preparation of bicontinuous nanoporous covalent frameworks, which are promising for caging active enzymes, is demonstrated. The frameworks have three‐ dimensionally continuous, hydrophilic pores with widths varying between 5 and 30 nm. Enzymes were infiltrated into the bicontinuous pore by applying a pressured enzyme solution. The new materials and methods allowed the amount of caged proteins to be controlled precisely. The resulting enzyme‐loaded framework films could be recycled many times with nearly no loss of catalytic activity. Entropic trapping of proteins by a bicontinuous pore with the right size distribution is an unprecedented strategy toward facile in vitro utilization of biocatalysts.