Silica encapsulated hemoglobin and myoglobin powders prepared by an aqueous fast-freezing technique

Autor:	W.J. DeSisto, Benjamin A. McCool, R. Cashon, G. Karles
Rok vydání:	2004
Předmět:	Aqueous solution Chromatography Silica gel Kinetics Buffer solution Liquid nitrogen Condensed Matter Physics Electronic Optical and Magnetic Materials chemistry.chemical_compound Myoglobin chemistry Materials Chemistry Ceramics and Composites Hemoglobin Silicic acid Nuclear chemistry
Zdroj:	Journal of Non-Crystalline Solids. 333:143-149
ISSN:	0022-3093
Popis:	Hemoglobin and myoglobin were encapsulated in silica gels and powders. Protein encapsulated powders were fabricated via the condensation of silicic acid around the protein, followed by a fast freezing with liquid nitrogen, and subsequent thawing. The fast-freezing technique led to high surface area stable silica encapsulated protein powders. Transmission UV–vis spectroscopy techniques were used to verify that neither protein was damaged during gelling or freezing processes. Both hemoglobin and myoglobin gels and powders retained their biological activity and were able to bind cyano ligands while in the oxidized Fe3+ state and carbon monoxy ligands while in the reduced Fe2+ state. Kinetics experiments showed that the rates of binding of CO and CN− to the proteins in the silica gel versus a buffer solution are decreased by 30–45%. This result was likely due to mass transfer effects associated with diffusion through the gel network. Hemoglobin/silica powders were successfully stabilized in the Fe2+ oxidation state by addition of the amino acid l-cysteine.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0e58e4426e99db1006744b20646079c3 https://doi.org/10.1016/j.jnoncrysol.2003.09.061 Zobrazit plný text záznamu Full Text from ScienceDirect