It has been suggested that structural proteins act as lignin nucleation sites in wildtype plants, perhaps via lignin-protein crosslinking. Furthermore, experiments with mutant plant lines have focused on secretion of novel proteins into plant cell walls, with the working hypothesis that cell wall physical and chemical properties may be altered, due at least in part to lignin-protein crosslinking. Yet in spite of this there have been few experiments demonstrating the propensity for lignin to crosslink with proteins, either in vitro or in vivo. Recently, we prepared lignin-protein linkages under biomimetic conditions by adding low molecular weight (tripeptides) and high molecular weight (gelatin) proteins to lignin dehydrogenation polymer (DHP) preparations. The DHPs were characterized using nuclear magnetic resonance, Fourier-transform infrared spectroscopy, and other techniques, and strong evidence for lignin-protein linkage formation was observed. We are currently searching for similar linkages in native lignins by growing Arabidopsis and isolating and characterizing lignin from the inflorescence stem. This work has provided and will continue to provide increased understanding of lignin-protein crosslinking mechanisms and how such linkages influence cell wall properties. Figure 1. <img src='https://acs-archive-assets2.s3.amazonaws.com/marm_2010/uploads/32442_jpg_structure.jpg' alt='' />

Formation of lignin-protein linkages in biomimetic systems and the implications of lignin-protein linkages in plants

247th National Meeting (2014)

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