Pepsin inactivation by inert gases

✍ Scribed by George M. Naimark; William A. Mosher

• Book ID: 103079245
• Publisher: Elsevier Science
• Year: 1952
• Tongue: English
• Weight: 40 KB
• Volume: 254
• Category: Article
• ISSN: 0016-0032
• DOI: 10.1016/0016-0032(52)90932-0

✦ Synopsis

It is well known that soluble globular proteins spread on quiescent gas-liquid interfaces to form two-dimensional monomolecular films of unfolded molecules. Since the bubbling of a gas through a liquid results in the rapid formation and collapse of gas-liquid interfaces, it is to be expected that such treatment would result in the denaturation and subsequent inactivation of protein enzymes.

It was found that the bubbling of argon, nitrogen or an argon-butane mixture through solutions of low concentration (0.2 per cent) of U.S.P. Merck Pepsin resulted in the rapid inactivation of the enzyme. An atmosphere of inert gas was not sufficient to cause inactivation. The inactivation caused by gas bubbling was not reversed by prolonged standing and was not due to the introduction of impurities by the gas.

We are led to conclude that gas bubbling provides gas-liquid interfaces upon which the enzyme spreads and forms monomolecular films. The collapse of the bubbles crushes the films and mechanically alters the protein structure. This type of enzyme inactivation is therefore the result of surface denaturation followed by the destruction of the formed films and is an irreversible reaction.