Adsorption of Ovalbumin Modified with Stearyl Groups on Hydrophobic Silica

Shlomo Magdassi, David Leibler, Sergei Braun

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Ovalbumin was modified to various degrees by acylation of lysine e-amino groups with stearyl residues. Adsorption isotherms of the modified ovalbumin on hydrophobic silica were obtained. It was found that increase in degree of modification resulted in increased amounts of adsorbed protein. At high modification degree (>40%), practically identical isotherms were obtained. The adsorption data were analyzed by using the Langmuir equation, and it appeared that increase in modification led to decrease in area per adsorbed protein molecule, while the adsorption constant remained unchanged.

Original languageAmerican English
Pages (from-to)376-378
Number of pages3
Issue number2
StatePublished - 1990
Externally publishedYes


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