Ectoenzyme Activity and Bacterial Secondary Production in Nutrient-Impoverished and Nutrient-Enriched Freshwater Mesocosms

• Published in: Microbial ecology 1993-03, Vol.25 (2), p.131-150
• Main Authors: Chróst, Ryszard J., Rai, Hakumat
• Format: Article
• Language: English
• Subjects: Aquatic environments; Bacteria; Bacterial biomass; Enzyme activity; Enzyme substrates; Enzymes; Kinetics; Lake water; Lakes; Phytoplankton
• ISSN: 0095-3628; 1432-184X
• DOI: 10.1007/bf00177191

This report presents results on relationships between the kinetics ( Vmaxand Km) of β-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 Vmaxof 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 Vmaxof GLCase and DOC and bacterial production in nutrient-impoverished and control (mesotrophic) enclosures. However, the Vmaxof 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.