Effect of lidocaine on ovalbumin and egg albumin foam stability

• Published in: Applied biochemistry and biotechnology 2003, Vol.105 -108 (1-3), p.905-911
• Main Authors: Burapatana, Vorakan, Butler, Ernest E, Chauhan, Gaurav, Hartig, Sean, Kincaid, Helen, Wang, Tong, Samsudin, Shayrizal, Tanner, Robert D
• Format: Article
• Language: English
• Subjects: Antifoaming Agents - chemistry; Antifoaming Agents - isolation & purification; Aqueous solutions; Bovine serum albumin; Decay rate; Drug Stability; Egg Proteins - chemistry; Egg Proteins - drug effects; Egg Proteins - isolation & purification; Foam separation; Foaming; Fractionation; Hydrophobicity; Lidocaine; Lidocaine - pharmacology; Organic wastes; Ovalbumin; Ovalbumin - chemistry; Ovalbumin - drug effects; Ovalbumin - isolation & purification; Proteins; Serum albumin; Stability analysis; Surface Tension
• ISSN: 0273-2289; 0273-2289; 1559-0291
• DOI: 10.1385/ABAB:108:1-3:905

Foam fractionation is a simple separation process that can remove and concentrate hydrophobic molecules such as proteins, surfactants, and organic wastes from an aqueous solution. Bovine serum albumin and ovalbumin have been widely used as model proteins due to their strong foaming potential and low price. Here, we study the effect of lidocaine on albumin foam, since drugs like lidocaine are known to bind with albumin. We observed that lidocaine not only enhances the amount of foam produced but also the stability of that foam as well. The foam stability was evaluated as the decay rate constant of the foam, determined from a change in height (or volume) of the foam over a given time period.