Ovalbumin, ovotransferrin, lysozyme: three model proteins for structural modifications at the air-water interface.

摘要: Structural modifications of ovalbumin, ovotransferrin, and lysozyme at the air−water interface have been investigated using SDS-PAGE, both intrinsic ANS fluorometry, circular dichroism experiments. Ovalbumin contact with an induced exposure aromatic residues, a slight decrease in α-helix structures (−1.7%), increase β-sheet (+3.4%) β-turn (+7.9%) structures. Moreover, these conformational changes led to formation insoluble polymers ovalbumin through intermolecular disulfide bonds. Ovotransferrin its surface hydrophobicity (+30%) secondary structure (−33% α-helices, +96.4% β-sheets, +13.2% β-turns, +21.2% random coils), characteristic major changes. On other hand, did not undergo any structural modification. These results clearly underscore that proteins are susceptible denaturation. Keywords: Ovalbumin; ov...