Unlike pectins from other origins, sugar beet pectin (SBP) acts as an emulsifier, a property which has been correlated to its more hydrophobic character and high protein content. In this work, we have investigated the structure of SBP at interfaces by atomic force microscopy (AFM). Three situations were studied: the mica/water, graphite/water, and air/water interface. For the latter, the interfacial film was transferred onto mica using the Langmuir-Blodgett method. While the adsorption of individual pectin chains on mica requires the addition of divalent cations, on graphite a thin layer containing amorphous areas and rodlike chains forms spontaneously. We suggest that the layer contains proteins and pectin chains which are bound to the graphite via CH-pi interactions. SBP adsorbed at the air/water interface forms an elastic layer, as evidenced by pendant drop and surface shear rheology measurements. AFM Images reveal the layer is crippled with holes and contains rodlike chains, suggesting that the pectin chains prevent the formation of a densely packed protein layer. Nevertheless, we show that the interfacial pectin film is more resistant to displacement by surfactants than a pure protein film, possibly because of the formation of linkages between the pectin chains. In contrast, alkali treatment of the pectin appears to remove the pectin chains from the air/water interface and leaves a Film that behaves similarly to pure protein. This work gives a new insight into the nanoscale organization of polysaccharides and polysaccharide-protein mixtures at macroscopic surfaces. The results gathered from the different interfaces studied permit a better understanding of the likely structure of SBP at the interface of emulsion droplets. Such knowledge might be used to modify rationally the pectin in order to improve its emulsifying properties, leading to broader commercial applications.