Aj. Thompson et Rl. Sinsabaugh, Matric and particulate phosphatase and aminopeptidase activity in limneticbiofilms, AQUAT MIC E, 21(2), 2000, pp. 151-159
Biofilms are a major nexus for biogeochemical transformations in inland wat
ers. A defining feature of biofilms is an extracellular polysaccharide matr
ix. One of the proposed functions of the matrix is retention of extracellul
ar enzymes. We investigated this function by following the kinetics of alka
line phosphatase (AP) and leucine aminopeptidase (LAP) in shaded and expose
d limnetic biofilms developed on glass slides. Organic matter (OM) accumula
tion and chlorophyll content were also measured. Biofilm was scraped from t
he slides and partitioned in matric and particulate (ectocellular plus detr
ital bound) fractions. In addition to enzyme activity, the matric fraction
was analyzed for carbohydrate and protein content. Over the May to October
study period, matric K-m values were significantly higher (by 30 to 50%) th
an particulate values for both enzymes in both treatments (n = 44). V-max v
alues were significantly higher in the particulate fraction for both enzyme
s in both treatments. Matric activity as a fraction of total activity avera
ged about 25 % (3:1 ratio particulate: matric) for both enzymes, suggesting
that the matrix was retaining enzymes. This was corroborated by principal
component analysis which in general tied matric enzyme activity with matric
carbohydrate and protein content and with OM accumulation and linked phosp
hatase activity to chlorophyll. There was no correlation between matric and
particulate enzyme activities and both varied widely. During periods of se
asonal turnover in dominant algal populations, matric activity exceeded par
ticulate. Matric enzymes appear to be a significant community resource whos
e activity may affect the dynamics of biofilm communities.