TY - JOUR
T1 - Synthesis and characterization of ordered mesoporous silicas for the immobilization of formate dehydrogenase (FDH)
AU - Pietricola, Giuseppe
AU - Tommasi, Tonia
AU - Dosa, Melodj
AU - Camelin, Enrico
AU - Berruto, Emanuele
AU - Ottone, Carminna
AU - Fino, Debora
AU - Cauda, Valentina
AU - Piumetti, Marco
N1 - Publisher Copyright:
© 2021
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2021/4/30
Y1 - 2021/4/30
N2 - This work studied the influence of the pore size and morphology of the mesoporous silica as support for formate dehydrogenase (FDH), the first enzyme of a multi-enzymatic cascade system to produce methanol, which catalyzes the reduction of carbon dioxide to formic acid. Specifically, a set of mesoporous silicas was modified with glyoxyl groups to immobilize covalently the FDH obtained from Candida boidinii. Three types of mesoporous silicas with different textural properties were synthesized and used as supports: i) SBA-15 (DP = 4 nm); ii) MCF with 0.5 wt% mesitylene/pluronic ratio (DP = 20 nm) and iii) MCF with 0.75 wt% mesitylene/pluronic ratio (DP = 25 nm). As a whole, the immobilized FDH on MCF0.75 exhibited higher thermal stability than the free enzyme, with 75% of residual activity after 24 h at 50 °C. FDH/MCF0.5 exhibited the best immobilization yields: 69.4% of the enzyme supplied was covalently bound to the support. Interestingly, the specific activity increased as a function of the pore size of support and then the FDH/MCF0.75 exhibited the highest specific activity (namely, 1.05 IU/gMCF0.75) with an immobilization yield of 52.1%. Furthermore, it was noted that the immobilization yield and the specific activity of the FDH/MCF0.75 varied as a function of the supported enzyme: as the enzyme loading increased the immobilization yield decreased while the specific activity increased. Finally, the reuse test has been carried out, and a residual activity greater than 70% was found after 5 cycles of reaction.
AB - This work studied the influence of the pore size and morphology of the mesoporous silica as support for formate dehydrogenase (FDH), the first enzyme of a multi-enzymatic cascade system to produce methanol, which catalyzes the reduction of carbon dioxide to formic acid. Specifically, a set of mesoporous silicas was modified with glyoxyl groups to immobilize covalently the FDH obtained from Candida boidinii. Three types of mesoporous silicas with different textural properties were synthesized and used as supports: i) SBA-15 (DP = 4 nm); ii) MCF with 0.5 wt% mesitylene/pluronic ratio (DP = 20 nm) and iii) MCF with 0.75 wt% mesitylene/pluronic ratio (DP = 25 nm). As a whole, the immobilized FDH on MCF0.75 exhibited higher thermal stability than the free enzyme, with 75% of residual activity after 24 h at 50 °C. FDH/MCF0.5 exhibited the best immobilization yields: 69.4% of the enzyme supplied was covalently bound to the support. Interestingly, the specific activity increased as a function of the pore size of support and then the FDH/MCF0.75 exhibited the highest specific activity (namely, 1.05 IU/gMCF0.75) with an immobilization yield of 52.1%. Furthermore, it was noted that the immobilization yield and the specific activity of the FDH/MCF0.75 varied as a function of the supported enzyme: as the enzyme loading increased the immobilization yield decreased while the specific activity increased. Finally, the reuse test has been carried out, and a residual activity greater than 70% was found after 5 cycles of reaction.
KW - Covalent immobilization
KW - Fluorescence microscopy
KW - Formate dehydrogenase
KW - Glyoxyl functionalization
KW - Ordered mesoporous silicas
UR - http://www.scopus.com/inward/record.url?scp=85101314026&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2021.02.114
DO - 10.1016/j.ijbiomac.2021.02.114
M3 - Article
AN - SCOPUS:85101314026
SN - 0141-8130
VL - 177
SP - 261
EP - 270
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -