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Characterization and Elimination of Undesirable Protein Residues in Plant Cell Wall Materials for Enhancing Lignin Analysis by Solution-State Nuclear Magnetic Resonance Spectroscopy

AuthorsKim, Hoon; Padmakshan, D.; Li, Yanding; Rencoret, Jorge CSIC ORCID; Hatfield, R.D.; Ralph, John
KeywordsAmino acids
Aromatic compounds
Magnetic resonance spectroscopy
Plant cell culture
Amino acid residues
Correlation peaks
Issue Date11-Dec-2017
PublisherAmerican Chemical Society
CitationBiomacromolecules 18(12) 4184-4195 (2017)
AbstractProtein polymers exist in every plant cell wall preparation, and they interfere with lignin characterization and quantification. Here, we report the structural characterization of the residual protein peaks in 2D NMR spectra in corn cob and kenaf samples and note that aromatic amino acids are ubiquitous and evident in spectra from various other plants and tissues. The aromatic correlations from amino acid residues were identified and assigned as phenylalanine and tyrosine. Phenylalanine's 3/5 correlation peak is superimposed on the peak from typical lignin p-hydroxyphenyl (H-unit) structures, causing an overestimation of the H units. Protein contamination also occurs when using cellulases to prepare enzyme lignins from virtually protein-free wood samples. We used a protease to remove the protein residues from the ball-milled cell walls, and we were able to reveal H-unit structures in lignins more clearly in the 2D NMR spectra, providing a better basis for their estimation
Description12 páginas.-- 5 figuras.-- 5 tablas.-- 74 referencias
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