계면에서의 단백질 흡착 기작을 연구하기 위하여 여러 단백질의 A/W 계면에서의 흡착이 조사되었다. BSA intermediates들의 흡착결과는 단백질 2차, 3차 구조가 계면에서의 흡착기작에 영향끼친 것을 나타냈으며, succinylated ${eta}-lactoglobulin$의 흡착에서는 순 음전하의 증가가 정전기적 상호작용에 영향끼침을 보여 주었다. 또한 ${eta}-casein$의 흡착은 물 구조를 파괴하는 chaotropic 염 존재하에서 흡착속도가 떨어지는 것을 시사했다.
To elucidate adsorption of proteins and examine the molecular behavior of protein molecules at interfaces, various proteins at the air-water interface were studied. The adsorption data of bovine serum albumin intermediates indicated that the conformational state of a protein played an important role in adsorption of proteins at interfaces. The adsorption behavior of succinylated beta-lactoglobulin indicated that the increase in the net negative charge of the protein significantly inflenced both the kinetics and thermodynamics of adsorption. The adsorption kinetics of beta-casein showed that the salt that induced break-down of water structure decreased the rate of adsorption.
