This article focuses on lysozyme inactivation at gas-liquid interfaces. Bubbling nitrogen in a lysozyme aqueous solution strongly enhances enzyme inactivation. At a 150-ml min(-1) flow rate, the half-life of lysozyme is 12 min while in the same conditions without bubbling no activity loss is observed after 8 h. Reported effects vary linearly with the interfacial area which shows that the inactivation is an interfacial mechanism. The inactivation induced by nitrogen bubbling strongly depends on temperature and pH acting on the adsorption process. This stud points out on the one hand the importance of controlling gas-liquid interfaces in bioreactors and on the other hand the potentialities of an inactivation process using gas-liquid interfaces.