TY - JOUR
T1 - Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
AU - Shortall, Kim
AU - Otero, Fernando
AU - Bendl, Simon
AU - Soulimane, Tewfik
AU - Magner, Edmond
N1 - Publisher Copyright:
© 2022 American Chemical Society.
PY - 2022/11/8
Y1 - 2022/11/8
N2 - Metal organic frameworks (MOFs) have been used to encapsulate an array of enzymes in a rapid and facile manner; however, the stability of MOFs as supports for enzymes has not been examined in detail. This study examines the stability of MOFs with different compositions (Fe-BTC, Co-TMA, Ni-TMA, Cu-TMA, and ZIF-zni) in buffered solutions commonly used in enzyme immobilization and biocatalysis. Stability was assessed via quantification of the release of metals by inductively coupled plasma optical emission spectroscopy. The buffers used had varied effects on different MOF supports, with incubation of all MOFs in buffers resulting in the release of metal ions to varying extents. Fe-BTC was completely dissolved in citrate, a buffer that has a profound destabilizing effect on all MOFs analyzed, precluding its use with MOFs. MOFs were more stable in acetate, potassium phosphate, and Tris HCl buffers. The results obtained provide a guide for the selection of an appropriate buffer with a particular MOF as a support for the immobilization of an enzyme. In addition, these results identify the requirement to develop methods of improving the stability of MOFs in aqueous solutions. The use of polymer coatings was evaluated with polyacrylic acid (PAA) providing an improved level of stability. Lipase was immobilized in Fe-BTC with PAA coating, resulting in a stable biocatalyst with retention of activity in comparison to the free enzyme.
AB - Metal organic frameworks (MOFs) have been used to encapsulate an array of enzymes in a rapid and facile manner; however, the stability of MOFs as supports for enzymes has not been examined in detail. This study examines the stability of MOFs with different compositions (Fe-BTC, Co-TMA, Ni-TMA, Cu-TMA, and ZIF-zni) in buffered solutions commonly used in enzyme immobilization and biocatalysis. Stability was assessed via quantification of the release of metals by inductively coupled plasma optical emission spectroscopy. The buffers used had varied effects on different MOF supports, with incubation of all MOFs in buffers resulting in the release of metal ions to varying extents. Fe-BTC was completely dissolved in citrate, a buffer that has a profound destabilizing effect on all MOFs analyzed, precluding its use with MOFs. MOFs were more stable in acetate, potassium phosphate, and Tris HCl buffers. The results obtained provide a guide for the selection of an appropriate buffer with a particular MOF as a support for the immobilization of an enzyme. In addition, these results identify the requirement to develop methods of improving the stability of MOFs in aqueous solutions. The use of polymer coatings was evaluated with polyacrylic acid (PAA) providing an improved level of stability. Lipase was immobilized in Fe-BTC with PAA coating, resulting in a stable biocatalyst with retention of activity in comparison to the free enzyme.
UR - http://www.scopus.com/inward/record.url?scp=85140965627&partnerID=8YFLogxK
U2 - 10.1021/acs.langmuir.2c01630
DO - 10.1021/acs.langmuir.2c01630
M3 - Article
C2 - 36286410
AN - SCOPUS:85140965627
SN - 0743-7463
VL - 38
SP - 13382
EP - 13391
JO - Langmuir
JF - Langmuir
IS - 44
ER -