Fluorescence properties of some farm wastes: implications for water quality monitoring

Some farm wastes have been analysed for their fluorescence properties using fluorescence excitation-matrix (EEM) spectroscopy. Farm wastes investigated were silage liquor, pig and cattle slurry, and sheep barn waste. All farm wastes exhibited high intensities of fluorescence that can be attributed to the protein tryptophan. Silage liquor was characterised by a very high fluorescence intensity and an initial tryptophan: fulvic-like fluorescence intensity ratio of > 20. Cattle and pig slurries exhibited a lower tryptophan: fulvic-like fluorescence intensity ratio (similar to2-5) and lower tryptophan fluorescence intensity, and tyrosine fluorescence was also observed. Sheep barn wastes had the lowest tryptophan: fulvic-like fluorescence intensity ratios (similar to0.5-4.0). Farm waste samples were reanalysed under controlled temperature conditions over a period of 50 days after sampling, to investigate the stability of their fluorescence properties. For silage liquor, tryptophan: fulvic-like fluorescence intensity ratios were observed to decrease with time, and were associated with a decrease in tryptophan fluorescence intensity, suggestive of clostridia breakdown of protein. For slurry samples, tryptophan: fulvic-like fluorescence intensity exhibited a more variable time-evolution, and tryptophan fluorescence intensity increased through time; the more complex fluorescence signal is due to the relatively heterogeneous nature of the slurry. Sheep barn waste samples exhibited more stable tryptophan: fulvic-like fluorescence intensity ratio and tryptophan intensities, suggesting these samples were more stable due to their greater age and decomposition. The ratios of tryptophan: fulvic-like fluorescence intensity observed from the farm wastes investigated are significantly higher than those observed in the majority of river waters, suggesting that farm waste pollution events could leave a signature in river waters due to their distinctively high protein fluorescence intensity. (C) 2001 Elsevier Science Ltd. All rights reserved.