Monitoring of adsorption behaviors of bovine serum albumin onto a stainless steel surface by the quartz crystal microbalance based on admittance analysis

• Published in: Bioscience, biotechnology, and biochemistry Vol. 81; no. 4; pp. 783 - 789
• Main Authors: Hagiwara, Tomoaki, Nattawut, Phosri, Shibata, Mario, Sakiyama, Takaharu
• Format: Journal Article
• Language: English
• Published: England Taylor & Francis 01.04.2017; Oxford University Press
• Subjects: Adsorption; Animals; bovine serum albumin; Cattle; dissipation factor; Hydrogen-Ion Concentration; protein adsorption; QCM-A; Quartz Crystal Microbalance Techniques; Serum Albumin, Bovine - chemistry; Solutions - chemistry; Stainless Steel - chemistry; stretched exponential function; Surface Properties; protein adsorption; QCM-A; stretched exponential function; dissipation factor; bovine serum albumin
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1080/09168451.2017.1281724

The adsorption process of bovine serum albumin (BSA) onto a stainless steel surface was investigated using the quartz crystal microbalance based on admittance analysis. The adhered mass change ∆m increased with time as a result of contacting the BSA solution, and considerably long period (>2 h) was required for the attainment of the asymptotic values of ∆m as well as dissipation factor ∆D. The relation between ΔD and Δm suggested that the layer of adsorbed BSA molecules became stiffer with increasing time at higher BSA concentration. The relation between Δm after 2 h and the final BSA concentration was described well by the Langmuir adsorption isotherm. However, the time course of Δm clearly deviated from the Langmuir adsorption model. The stretched exponential function model described the time course of Δm well although it was an empirical one.