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The adsorption of globular proteins, bovine serum albumin and b-lactoglobulin, on poly-L-lysine–furcellaran multilayer

Year: 2006

Journal: Carbohydrate Polymers 65 (2006) 235–242, 20100827

Authors: Laos K., Parker R., Moffat J., Wellner N., Ring S.G.

Last authors: S.G. Ring

Organizations: Institute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, UK

Country: UK, United Kingdom

The formation of multilayer films of poly-L-lysine (PLL) and furcellaran was investigated using surface plasmon resonance (SPR), quartz crystal microbalance with dissipation monitoring (QCM-D) and Fourier transform infrared spectroscopy with attenuated total reflection (FTIR-ATR). The progressive form of the growth of mass of polymer deposited for the multilayer was consistent with the ability of the PLL to diffuse within the furcellaran layer. Using the same experimental approaches, the pH-dependent adsorption of the globular proteins, bovine serum albumin (BSA) and b-lactoglobulin (BLG), to the PLL–furcellaran multilayers was also examined. Substantial adsorption was observed even at pH’s above the isoelectric point where the net charge on the protein was of the same sign as that of the furcellaran.