TY - JOUR
T1 - Enhanced Activity of Enzymes Encapsulated in Hydrophilic Metal–Organic Frameworks
AU - Liang, Weibin
AU - Xu, Huoshu
AU - Carraro, Francesco
AU - Maddigan, Natasha K.
AU - Li, Qiaowei
AU - Bell, Stephen G.
AU - Huang, David M.
AU - Tarzia, Andrew
AU - Solomon, Marcello B.
AU - Amenitsch, Heinz
AU - Vaccari, Lisa
AU - Sumby, Christopher J.
AU - Falcaro, Paolo
AU - Doonan, Christian J.
PY - 2019/1/12
Y1 - 2019/1/12
N2 - Encapsulation of biomacromolecules in metal–organic frameworks (MOFs) can preserve biological functionality in harsh environments. Despite the success of this approach, termed biomimietic mineralization, limited consideration has been given to the chemistry of the MOF coating. Here we show that enzymes encapsulated within hydrophilic MAF-7 or ZIF-90 retain enzymatic activity upon encapsulation and when exposed to high temperatures, denaturing or proteolytic agents, and organic solvents, whereas hydrophobic ZIF-8 affords inactive catalase and negligible protection to urease.
AB - Encapsulation of biomacromolecules in metal–organic frameworks (MOFs) can preserve biological functionality in harsh environments. Despite the success of this approach, termed biomimietic mineralization, limited consideration has been given to the chemistry of the MOF coating. Here we show that enzymes encapsulated within hydrophilic MAF-7 or ZIF-90 retain enzymatic activity upon encapsulation and when exposed to high temperatures, denaturing or proteolytic agents, and organic solvents, whereas hydrophobic ZIF-8 affords inactive catalase and negligible protection to urease.
KW - MOFs
KW - biomineralization
KW - Enzyme immobilization
KW - encapsulation
UR - http://www.scopus.com/inward/record.url?scp=85061255882&partnerID=8YFLogxK
U2 - 10.1021/jacs.8b10302
DO - 10.1021/jacs.8b10302
M3 - Article
SN - 0002-7863
VL - 141
SP - 2348
EP - 2355
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 6
ER -