Protein-surfactant interactions are the focus of extensive research due to their many applications in food technology and detergent industry. In this work, we investigate the interaction between bovine serum albumin (BSA) and five relevant surfactants to the cleaning industry, which differ in head group charge, namely: sodium alkyl ether sulphate (C12-C14 AE3S), Cocoamidopropyl amine-oxide (CapAO), alkyl dimethyl amine oxide (C12C14AO), octaethylene glycol monodecyl ether (C10EO8) and didecyldimethylammonium chloride (DDAC). The results collected with fluorescence emission spectroscopy highlight zwitterionic and nonionic surfactants have the lowest affinity for the protein, as their interaction does not result in protein denaturation. Instead, higher and mutually close binding constants are found for AE3S (anionic) and DDAC (cationic) due to the presence of electrostatic interactions between the surfactant heads and the charged residues of BSA. AE3S leads to irreversible protein unfolding. The case of DDAC is more complex and has been studied through a combination of fluorescence, DLS, PGSE-NMR and zeta-potential measurements. At low concentration DDAC binding neutralizes negatively charged residues present in BSA, causing a reversible flocculation of BSA after the isoelectric point
Binding isotherms of surfactants used in detergent formulations to bovine serum albumin
Helena Mateos;Giuseppe colafemmina;Gerardo Palazzo
2020-01-01
Abstract
Protein-surfactant interactions are the focus of extensive research due to their many applications in food technology and detergent industry. In this work, we investigate the interaction between bovine serum albumin (BSA) and five relevant surfactants to the cleaning industry, which differ in head group charge, namely: sodium alkyl ether sulphate (C12-C14 AE3S), Cocoamidopropyl amine-oxide (CapAO), alkyl dimethyl amine oxide (C12C14AO), octaethylene glycol monodecyl ether (C10EO8) and didecyldimethylammonium chloride (DDAC). The results collected with fluorescence emission spectroscopy highlight zwitterionic and nonionic surfactants have the lowest affinity for the protein, as their interaction does not result in protein denaturation. Instead, higher and mutually close binding constants are found for AE3S (anionic) and DDAC (cationic) due to the presence of electrostatic interactions between the surfactant heads and the charged residues of BSA. AE3S leads to irreversible protein unfolding. The case of DDAC is more complex and has been studied through a combination of fluorescence, DLS, PGSE-NMR and zeta-potential measurements. At low concentration DDAC binding neutralizes negatively charged residues present in BSA, causing a reversible flocculation of BSA after the isoelectric pointFile | Dimensione | Formato | |
---|---|---|---|
1-s2.0-S0927775720303940-main.pdf
non disponibili
Descrizione: Articolo in rivista
Tipologia:
Documento in Versione Editoriale
Licenza:
NON PUBBLICO - Accesso privato/ristretto
Dimensione
2.51 MB
Formato
Adobe PDF
|
2.51 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
Binding isotherms of surfactants used in detergent formulations to bovine serum albumin.pdf
accesso aperto
Descrizione: Articolo in pre print
Tipologia:
Documento in Pre-print
Licenza:
Copyright dell'editore
Dimensione
732.8 kB
Formato
Adobe PDF
|
732.8 kB | Adobe PDF | Visualizza/Apri |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.