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Ectoenzyme activity and bacterial secondary production in nutrient-impoverished and nutrient-enriched freshwater mesocosms
Authors:Ryszard J. Chróst  Hakumat Rai
Affiliation:(1) Max-Planck Institute for Limnology, 165, DW-2320 Plön, Germany;(2) Present address: Institute of Microbiology University of Warsaw, ul. Nowy "Sacute"wiat 67, 00-927 Warsaw, Poland
Abstract:This report presents results on relationships between the kinetics (Vmax and Km) of beta-glucosidase (GLCase) and aminopeptidase (AMPase) activity, and dissolved organic carbon (DOC) and bacterial secondary production in freshwater mesocosms of differing degrees of eutrophication. These relationships varied in different mesocosms and depended on the trophic status of water and the exudation rates of organic carbon (EOC) by phytoplankton. Close coupling of bacterial production to Vmax of GLCase activity was observed only in nutrient-enriched mesocosms. The relationship between GLCase and DOC content was also significant in enriched water. There was no correlation between the Vmax, of GLCase and DOC and bacterial production in nutrient-impoverished and control (mesotrophic) enclosures. However, the Vmax of AMPase correlated well to DOC and bacterial production in these mesocosms. AMPase activity did not correlate with DOC and bacterial production in nutrient-impoverished mesocosms. There was no relationship between bacterial biomass and enzyme activity in all studied mesocosms. Comparison of the rates of phytoplankton production of EOC and rates of the bacterial organic carbon demand (BOCD) in nutrient-impoverished mesocosms showed that EOC flux constituted, on average, 90% of BOCD. However, in nutrient-enriched mesocosms EOC contributed only, on average, 27% to the BOCD; thus, in these mesocosms, bacteria were probably organic-carbon limited. It is hypothesized that to bypass substrate limitation, bacteria produced GLCase and AMPase. These enzymes had a high specific activity and high affinity to their substrates and efficiently hydrolyzed polysaccharides and proteins, thereby supplying microorganisms with readily utilizable products of enzyme catalysis.Offprint requests to: R.J. Chróst.
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