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- W2375619523 abstract "Hydrophobins are small secreted proteins produced by filamentous fungi,which can form an amphipathic membrane at various surfaces.Hydrophobins have been considered as excellent substrates for protein immobilization.However,the driven force for protein adsorption on hydrophobin surface is not clear.In this work,we systematically investigated the protein adsorption on hydrophobins at different pH and ionic strength.Firstly,the adsorption of class Ⅰ hydrophobin HGFI and class Ⅱ hydrophobin HFBI on the surfaces of polystyrene were investigated via quartz crystal microbalance with dissipation monitoring(QCM-D) at different pH and ionic strength.The results show that both pH and ionic strength have greater impacts on the adsorption of HGFI on polystyrene than that of HFBI.Moreover,HGFI can form soft films on the polystyrene,whereas HFBI formed very rigid films under the same conditions.The adsorption of BSA and avidin on the HGFI and HFBI were further investigated by using QCM-D at the same pH and ionic strength.The results indicate that adsorptions of BSA and avidin on the HGFI and HFBI are dramatically affected by both pH and ionic strength,suggesting that the major driving force dominating the protein adsorption on hydrophobin is the electrostatic force.This study provides a theoretical guide for a controllable immobilization of a protein on a hydrophobin surface." @default.
- W2375619523 created "2016-06-24" @default.
- W2375619523 creator A5078046664 @default.
- W2375619523 date "2010-01-01" @default.
- W2375619523 modified "2023-09-25" @default.
- W2375619523 title "Adsorption of Protein on Hydrophobin Surface Driven by Electrostatic Force" @default.
- W2375619523 hasPublicationYear "2010" @default.
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