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Appl Biochem Biotechnol ; 193(4): 1072-1085, 2021 Apr.
Article in English | MEDLINE | ID: mdl-33405010

ABSTRACT

MCM-41 and MCM-48 with niobium were successfully synthesized using 1-tetradecyl-3-methylimidazolium chloride ([C14MI]Cl) as a structure-directing agent. The best Si/Nb molar ratio was chosen (Si/Nb = 20) and the CALB enzyme was immobilized in situ in the synthesized Nb-MCM. SEM micrographs showed the formation of very regular spherical agglomerates with a diameter between 0.25 and 0.75 µm. The material presented a surface area of 954 and 704 m2/g and a pore volume of 0.321 and 0.286 cm3/g, for Nb-MCM-41 and Nb-MCM-48, respectively. Also, both materials showed a pore size of 2.261 nm. The number of recycles obtained for the CALB enzyme immobilized in Nb-MCM-41 and Nb-MCM-48 was 26 recycles with a residual activity of 49.62% and 16 recycles with a residual activity of 53.01%, respectively. For both materials, enzymatic activity remained stable for 5 months of storage at room temperature and refrigeration. The supports were able to catalyze the esterification reaction at 40, 60, and 80 °C, showing industrial application in reactions that require high temperatures. This methodology allows the preparation of new highly active and selective enzyme catalysts using niobium and [C14MI]Cl. Also, the new materials can provide greater viability in processes, ensuring a longer service life of catalysts. Graphical abstract.


Subject(s)
Enzymes, Immobilized/chemistry , Lipase/chemistry , Niobium/chemistry , Silicon Dioxide/chemistry , Catalysis , Esterification , Hydrogen-Ion Concentration
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