The adsorption of the two main proteins in soy, glycinin and �-conglycinin, was studied by using quartz crystal microgravimetry, surface plasmon resonance, circular dichroism, and water contact angle measurements.  The amounts of both globulins adsorbed from aqueous solutions of various pH and ionic strength were measured onto lignin and cellulose. While the adsorption on cellulose was drastically affected by salt addition little or no change was observed in the case of lignin substrates. In addition, adsorption of denatured proteins (mercaptoethanol or urea) was reduced (�50%). These observations indicate the relevance of hydrophobic interactions and the breaking the disulfide linkages in the macromolecules. Water contact angle measurements before and after protein adsorption supported our interpretation of the results in terms of the contribution of hydrophobic and hydrophilic aminoacids interacting with lignin and cellulose, respectively.

Surface modification of cellulose and lignin by adsorption of soy proteins

243rd National Meeting (2012)

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