Several characteristics of β-lactoglobulin (BLG) layers adsorbed at the air/water interface exhibit a strong pH dependence, but our knowledge on the underlying structure-property relations is still fragmental. Here, we therefore extend our recent studies by neutron reflectometry (NR) and provide a comprehensive overview through direct measurements of the surface excess Γ and the layers' molecular structure. This enables comparison with available literature data to draw general conclusions. The NR experiments were performed at various pH values and within a wide range of protein concentrations, CBLG. Adsorption kinetics measurements in air-contrast-matched-water and over a narrow Qz range enabled direct quantification of the dynamic surface excess Γ(t) and are found to be consistent with ellipsometry data. Near the isoelectric point, pI, the rates of adsorption and Γ are maximal but only at sufficiently high CBLG. NR data collected over a wider Qz range and in two aqueous isotopic contrasts revealed the structure of adsorbed BLG layers at a steady state close to equilibrium. Independent of the pH, BLG was found to form dense monolayers with average thicknesses of 1.1 nm, suggesting flattening of the BLG globules upon adsorption as compared with their bulk dimensions (≈3.5 nm). Near pI and at sufficiently high CBLG, a thick (≈5.5 nm) but looser secondary sublayer is additionally formed adjacent to the dense primary monolayer. The thickness of this sublayer can be interpreted in terms of disordered BLG dimers. The results obtained and notably the specific interfacial structuring of BLG near pI complement previous observations relating the impact of solution pH and CBLG on other interfacial characteristics such as surface pressure and surface dilational viscoelasticity modulus.