Ovalbumin, Ovotransferrin, Lysozyme: Three Model Proteins for Structural Modifications at the Air−Water Interface - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Agricultural and Food Chemistry Année : 2003

Ovalbumin, Ovotransferrin, Lysozyme: Three Model Proteins for Structural Modifications at the Air−Water Interface

Résumé

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

Dates et versions

hal-01347886 , version 1 (21-07-2016)

Identifiants

Citer

Valérie Lechevalier-Datin, Thomas Croguennec, Stephane Pezennec, Catherine Guérin-Dubiard, Maryvonne Pasco, et al.. Ovalbumin, Ovotransferrin, Lysozyme: Three Model Proteins for Structural Modifications at the Air−Water Interface. Journal of Agricultural and Food Chemistry, 2003, 51 (21), pp.6354-6361. ⟨10.1021/jf034184n⟩. ⟨hal-01347886⟩
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