-We studied the structural behaviour and foaming properties of whey proteins under the effects of spray-drying in a co-current configuration. We used two different inlet/outlet air temperatures (170/85• C or 260/138• C, respectively), the other operating conditions being unchanged. Using different characterisation techniques, we showed that both whey proteins (WP-P 85 and WP-P 138 ) which were submitted to hydro-thermal treatments under mild and high air processing conditions behaved differently from untreated proteins (WP-L). As expected, WP-P 138 powder exhibited lower moisture and free lactose contents, a higher particle internal porosity, and a thinner particle wall thickness than the WP-P 85 powder. The conformational stability of whey proteins, obtained by dilution of untreated whey proteins (WP-L) and dispersions of the two spray-dried powders (WP-P 85 and WP-P 138 ), were compared. Whey proteins in the WP-P 138 powder showed a red-shift in the tryptophan emission wavelength, the appearance of a newly created fluorescent compound at 420 nm, contrary to untreated and WP-P 85 whey proteins. In addition, we observed formation of a higher proportion of covalently-bound aggregates (11% in WP-P 138 , instead of 5% in WP-P 85 ) and a decrease in conformational stability against re-heating (∼50% s in WP-P 138 , instead of ∼30% in WP-P 85 ) compared with untreated WP-L solution. Finally, combination of continuous measurements of foam volume (by an on-line video camera) and liquid (by conductivity) entrained in a column foam during its formation by air injection, in parallel with automatic acquisition of videofoam images during the destabilisation step, showed that solution of WP-P 138 spray-dried powder, obtained using the highest air temperature conditions, has higher foaming properties than WP-P 85 and WP-L solutions. • C et 260/138• C, respectivement), les autres conditions opératoires étant inchangées. Par application de différentes techniques de caractérisa-tion, nous avons montré que les protéines (WP-P 85 et WP-P 138 ) qui ont subi des traitements hydrothermiques à température d'air modérée et sévère, respectivement, se comportent différemment des protéines (WP-L) contenues dans les solutions avant séchage. Comme attendu, la poudre contenant les protéines WP-P 138 présente des taux d'humidité et de lactose libre plus faibles, un taux de porosité interne plus important, et une épaisseur de paroi plus faible. L'étude spectrofluorimétrique des protéines, contenues dans des dispersions dans l'eau distillée des poudres issues des deux conditions de séchage, indique que pour les protéines WP-P 138 , et contrairement aux protéines WP-L et WP-P 85 , la longueur d'onde maximum d'émission de fluorescence du tryptophane présente un déplacement vers le rouge, ainsi que l'apparition de nouveaux composés qui fluorescent avec une longueur d'onde maximum d'émission à 420 nm. D'autre part, nous avons observé une plus forte proportion d'agrégats covalents (11 % pour WP-P 138 au lieu de 5 % pour WP-P 85 ), ainsi qu'...