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Protein Adsorption onto Metal Oxide Materials in White Wine Model Systems
Author(s) -
Pachova V.,
Ferrando M.,
Güell C.,
Lóapez F.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb09511.x
Subject(s) - adsorption , chemistry , egg white , bovine serum albumin , protein adsorption , oxide , ovalbumin , metal , zirconium , langmuir adsorption model , chromatography , zirconium oxide , inorganic chemistry , cubic zirconia , nuclear chemistry , organic chemistry , ceramic , immune system , immunology , biology
Three standard proteins—bovine serum albumin (BSA), ovalbumin (OVAL), and lysozyme (LYS)—were used to evaluate metal oxide adsorption isotherms. The isotherms of BSA adsorbed on powdered ZrO 2 and those of LYS adsorbed on pellets of ZrO 2 or spheres of Al 2 O 3 at pH 3.5 were well fitted by the Langmuir model. The adsorption curve of OVAL on powdered ZrO 2 showed an inflection point at the same pH. The adsorption curves obtained from the other systems (protein‐metal oxide) were unfavorable. Protein adsorption of a white wine onto zirconium oxide showed adsorption selectivity. Zirconium had a preference for removing the unstable proteins, and that it could be used to stabilize white wines.