Adsorption of Protein onto Stainless-Steel Surfaces

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The adsorption of bovine serum albumin (BSA) and gelatin onto stainless-steel surfaces was studied as a function of pH, using nonporous stainless-steeel particles. The net charge equivalents of BSA and gelatin increased with increasing difference in pH values from the isoelectric points (I.E.P.'s) of the respective proteins, accompanied by charge-induced molecular expansion. BSA and gelatin adsorbed spontaneously on positively and negatively charged stainless-steel surfaces, even though the proteins had the ame sign of charge as that of the stainless-steel surfaces. Adsorption isotherms similar to Langmuir-type ones with saturation plateaus were constructed for BSA and gelatin in a pH range of 3.2 to 8.0. The plateau values varied with pH, giving maxima around the I.E.P.'s of BSA and gelatin. Calculation of saturation area per BSA molecule adsorbed on stainless-steel surfaces suggests that the net charge on protein molecules is a key factor determining the packing density of protein molecules in the adsorbed layer. An increase in ionic strength from 10^<-3> to 10^<-1> resulted in a significant increase in the adsorbed amount of BSA but a slight decrease in that of gelatin in the isoelectric regions of the proteins. The adsorption of BSA onto stainless-steel surfaces was markedly enhanced at temperatures above 50℃, beyond which BSA was progressively denatured. On the other hand, the adsorbed amount of gelatin decreased gradually from 40 to 80℃. It is concluded that the adsorption behavior of proteins at stainless steel-liquid interfaces was mainly governed by the properties of solute protein molecules under changing environmental conditions, rather than by the nature of the stainless-steel surfaces.
社団法人日本生物工学会の論文
1995-07-25

Adsorption of Protein onto Stainless-Steel Surfaces

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