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    On the Surface Interactions of Proteins with Lignin

    Year: 2013

    Journal: ACS Appl. Mater. Interfaces, 2013, 5 (1), pp 199–206, 20130403

    Authors: Carlos Salas 1 2, Orlando J. Rojas * 1 3 , Lucian A. Lucia 1, Martin A. Hubbe 1, and Jan Genzer 3

    Last authors: Jan Genzer

    Organizations: 1 Department of Forest Biomaterials and §Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695, United States 2 Department of Chemical Engineering, Universidad de Los Andes, Mérida 5101, Venezuela 3 School of Chemical Technology, Department of Forest Products Technology, Aalto University, 00076 Aalto, Finland

    Country: USA, US, United States, United States of America, America, Venezuela, Finland

    Lignins are used often in formulations involving proteins but little is known about the surface interactions between these important biomacromolecules. In this work, we investigate the interactions at the solid–liquid interface of lignin with the two main proteins in soy, glycinin (11S) and β-conglycinin (7S). The extent of adsorption of 11S and 7S onto lignin films and the degree of hydration of the interfacial layers is quantified via Quartz crystal microgravimetry (QCM) and surface plasmon resonance (SPR). Solution ionic strength and protein denaturation (2-mercaptoethanol and urea) critically affect the adsorption process as protein molecules undergo conformational changes and their hydrophobic or hydrophilic amino acid residues interact with the surrounding medium. In general, the adsorption of the undenatured proteins onto lignin is more extensive compared to that of the denatured biomolecules and a large amount of water is coupled to the adsorbed molecules. The reduction in water contact angle after protein adsorption (by 40° and 35° for undenatured 11S and 7S, respectively) is explained by strong nonspecific interactions between soy proteins and lignin.