Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 10, Issue 5, Pages 453-469Publisher
ELSEVIER
DOI: 10.1016/S1381-1177(99)00123-X
Keywords
mesoporous molecular sieves; enzyme immobilization; cytochrome c; MCM-48; SBA-15; Nb-TMS4
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The immobilization of cytochrome c into the mesoporous moleclar sieves MCM-48 (Mobil Composition of Matter) and SBA-15 (Santa Barbara Amorphous), as well as the layered niobium oxide Nb-TMS4 (Niobium Transition Metal Oxide Molecular Sieve) is described. The cytochrome c loading was influenced by the molecular sieve structure, i.e., one-dimensional vs. three-dimensional. Cytochrome c immobilization was accomplished by absorption into the molecular sieves followed by silylation of the pore openings. The molecular sieves containing cytochrome c were characterized by X-ray diffraction (XRD), scanning electron microscopy (SEM), UV/Vis, and FT-IR spectroscopy. The protein was found to be stable in the molecular sieve under conditions that would denature the protein in solution. The immobilized cytochrome c retained its redox activity following immobilization for several months as demonstrated by cyclic voltammetry (CV). (C) 2000 Elsevier Science B.V. All rights reserved.
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