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- Title
A 1-year study of the activities of seven hydrolases in a communal wastewater treatment plant: trends and correlations.
- Authors
Kreutz, Jennifer; Böckenhüser, Ina; Wacht, Marion; Fischer, Klaus
- Abstract
The activities of seven hydrolytic enzymes (L-alanine aminopeptidase, esterase, α-and β-glucosidase, phosphomonoesterase, phosphodiesterase, sulfatase) were monitored during 1 year in parallel and serial treatment units of the biological stage of a communal wastewater treatment plant. The spatial homogeneity of enzyme activities was high (coefficients of variation <10 % for the entire treatment stage). A significant difference between aerated and stirred tanks was not observed. Temperature seemed not to exert a direct influence. Long periods with comparably constant activities were interrupted by a few strong, short-time rises. The mean enzyme activities followed the sequence sulfatase < α-glucosidase < phosphodiesterase ≈ β-glucosidase≈esterase < phosphomonoesterase < L-alanine aminopeptidase. The enzyme activities correlated among themselves at different levels. Very strong ( r > 0.8) and highly significant ( p < 0.01) correlations between the activities of both glucosidases, both phosphoesterases, and between phosphomonoesterase and both glucosidases were ascertained, pointing to the importance of substrate specificity and similarity of metabolic functions. Moderate and strong activity correlations with various wastewater constituents and with process parameters, e.g., concentrations, loads and eliminated amounts of phosphorous, TOC concentrations and loads of the plant effluent, dry matter content of activated sludge, and sludge volume, were found. The esterase activity was least correlated with other enzymes and often showed deviating dependencies on process parameters, raising questions concerning its appropriateness as a sum parameter for enzymatic and heterotrophic activity.
- Subjects
HYDROLASES; ACTIVATED sludge process; ACYLPEPTIDE hydrolase; WASTEWATER treatment; GLUCOSIDASES
- Publication
Applied Microbiology & Biotechnology, 2016, Vol 100, Issue 15, p6903
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-016-7540-6