Figure 5
(Panel A) Overlay of 1H, 1H COSY (correlated spectroscopy; green cross peaks), 1H, 1H TOCSY (total correlated spectroscopy; coloured cross peaks) and (panel B) 1H, 13C DEPT HSQC (distortionless enhancement by polarization transfer; heteronuclear single quantum coherence) nuclear magnetic resonance (NMR) spectra (colour code: purple, CH123; blue, CH; green, CH2; red, CH3) of the Niltre first effluent DOM (NiEf1) aliphatic section, with cross peaks of proteinaceous amino acids (see attendant single letter code) in proteins following alanine, (A) annotated according to position and carbon multiplicity. (Panel A): upper left half: amino acid-derived COSY cross peaks according to positioning in peptides (blue squares); lower right half: amino acid-derived TOCSY cross peaks according to individual amino acids (individual grey symbols). (Panel B): 1H, 13C DEPT HSQC NMR spectrum; colour code: purple, CH123; blue, CH; green, CH2; red: CH357,58. Orange box denotes the section of OCHn cross peaks59 (cf. Figs 3A and S2). e1: aromatic methyl esters, e2: aliphatic methyl esters, e3: aromatic methyl esters, e4: aliphatic methyl ethers, e5: oxyomethylene OCH2, largely from carbohydrates. The abundance follows: e5 ≫ e1 ≈ e2: > e3 ≫ e4. Projection 1H NMR spectra on top (F2 dimension) represent the Niltre first effluent DOM NiEf1 (black) and difference 1H NMR spectra (1st effluent minus pristine; NiEf1 – NiCo) Niltre first effluent DOM (cf. Fig. S9), whereas multiplicity edited 13C NMR subspectra (F1 dimension) are shown for panel B (cf. Fig. S10).
