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In this paper the surface activity of protein mucin at solution/air interface has been studied. The experiments of the adsorbed protein at solution/air interface have been carried out with a range of protein concentrations at a defined pH. The adsorption of the protein to solid surfaces and the degree of hydrophobicity at solid/solution interface of mucin have been evaluated at different pH and in the presence of Hofmeister electrolyte. The results from these studies have been further substantiated by surface potential measurements of mucin covered surface on stainless steel. Quartz crystal microbalance (QCM) has been used to follow the protein adsorption kinetics from solution to solid surface. The results from these measurements show that the adsorption behavior has a remarkable dependence on the degree of maximum coverage and is almost independent of the ionic strength. Other characteristic features such as maximum adsorption values at the protein isoelectric point (IEP4.7) and low-affinity isotherms that showed surface saturation even under unfavorable electrostatic conditions have been observed. The amount of mucin adsorbed in the presence of electrolytes has been estimated using electron spectroscopy for chemical analysis (ESCA). The study clearly shows that there exists an inverse relationship between the hydrophobicity and surface tension of the protein and also on the hydrated radius of Hofmeister electrolyte used.