of glucosamine compounds, again, deviated from this pattern in that it only correlated
with bacterial numbers at the station Hauptpost.
In both areas of investigation a wide range of EEA’s was observed over the year. (Tab. 3).
Generally an increase in V m of EEA’s was found in enclosed inshore waters. At the
polluted inner fjord station annual average values of V
m
of protease were 1.6 times higher
than at the offshore station. The corresponding values were 3.1 for V
m
of α-glucosidase,
1.5 for glucosaminidase and 1.9 for phosphatase (c.f. Table 4). This increase was proportional to that of total bacterial number, uptake velocity of leucine and chlorophyll a
content of the water. Saprophytic bacteria numbers did not fit this correlation. For the
hydrolyzation rates (HR, % h -1 ) of the different MUF-substrates this uniformity of
response could not be detected. The hydrolyzation rates for MUF-leucine substrate
analogues were 3 times higher, and those for MUF- phosphate were 5 times higher at the
offshore station. In contrast HR for MUF-α-glucoside substrate analogues were 5.5 times
smaller and those for MUF-glucosaminide were 10 times smaller at the offshore station
than at the polluted inshore station.
Parameter
Station Haup
Minimum
post (inshore)
Maximum
Station Feuers
Minimum
chiff (offshore)
Maximum
1) Saprophytes
2,600
283,300
100
12,600
2) AODC
1.4
9.6
0.5
2.5
3) V m - leucine uptake
0.01
0.3
0.001
0.09
4) TR - leucine
0.25
12.1
0.22
8.9
5) V
m
MUF-leucine
0.93
22.4
0.29
14.1
6) V m MUF-a-glucoside
0.02
1.06
0.01
0.17
7) V m MUF-glucosaminide
0.07
0.55
0.08
0.53
8) V m MUF-phosphate
0.004
0.16
0.002
0.07
9) HR MUF-leucine
0.06
2.2
0.08
17.8
10) HR MUF-glucoside
0.002
14.0
0.001
4.3
11) HR MUF-glucosaminide
0.006
2.7
0.001
0.13
12) HR MUF-phosphate
0.026
0.53
0.01
8.3
13) Chl. a
0.34
18.8
0.74
9.3
Units 1) saprophytes ml -1
2) total bacteria numbers ml -1 x 10 6 ; 3) ug C l -1 h-1 ; 4) % h-1 ; 5) - 7) µg Cl -1 h'1 ; 8) µM l-1 h-1 ; 9) - 12) %
h -1 ; 13)µg l -1
Table 3 : Extreme values of different parameters obtained from 12 monthly investigations.
Though pool sizes of polymers (including oligomers) and of monomers of the different
substrates investigated are not known, some indication for the mechanism of equilibration between these pools may arise from the comparison of hydrolyzation rate (HR, %
h'
1 ) of the directly available part of the polymer pool and the turnover rate (TR, % h'1 ) of
the corresponding monomer pool. However, one must bear in mind, that the polymer
hydrolyzation rate as measured via MUF-substrates will, at best, provide a relative
measure of that part of the polymer pool which is exposed to enzymatic splitting from the
end points of the macromolecules.
124
with bacterial numbers at the station Hauptpost.
In both areas of investigation a wide range of EEA’s was observed over the year. (Tab. 3).
Generally an increase in V m of EEA’s was found in enclosed inshore waters. At the
polluted inner fjord station annual average values of V
m
of protease were 1.6 times higher
than at the offshore station. The corresponding values were 3.1 for V
m
of α-glucosidase,
1.5 for glucosaminidase and 1.9 for phosphatase (c.f. Table 4). This increase was proportional to that of total bacterial number, uptake velocity of leucine and chlorophyll a
content of the water. Saprophytic bacteria numbers did not fit this correlation. For the
hydrolyzation rates (HR, % h -1 ) of the different MUF-substrates this uniformity of
response could not be detected. The hydrolyzation rates for MUF-leucine substrate
analogues were 3 times higher, and those for MUF- phosphate were 5 times higher at the
offshore station. In contrast HR for MUF-α-glucoside substrate analogues were 5.5 times
smaller and those for MUF-glucosaminide were 10 times smaller at the offshore station
than at the polluted inshore station.
Parameter
Station Haup
Minimum
post (inshore)
Maximum
Station Feuers
Minimum
chiff (offshore)
Maximum
1) Saprophytes
2,600
283,300
100
12,600
2) AODC
1.4
9.6
0.5
2.5
3) V m - leucine uptake
0.01
0.3
0.001
0.09
4) TR - leucine
0.25
12.1
0.22
8.9
5) V
m
MUF-leucine
0.93
22.4
0.29
14.1
6) V m MUF-a-glucoside
0.02
1.06
0.01
0.17
7) V m MUF-glucosaminide
0.07
0.55
0.08
0.53
8) V m MUF-phosphate
0.004
0.16
0.002
0.07
9) HR MUF-leucine
0.06
2.2
0.08
17.8
10) HR MUF-glucoside
0.002
14.0
0.001
4.3
11) HR MUF-glucosaminide
0.006
2.7
0.001
0.13
12) HR MUF-phosphate
0.026
0.53
0.01
8.3
13) Chl. a
0.34
18.8
0.74
9.3
Units 1) saprophytes ml -1
2) total bacteria numbers ml -1 x 10 6 ; 3) ug C l -1 h-1 ; 4) % h-1 ; 5) - 7) µg Cl -1 h'1 ; 8) µM l-1 h-1 ; 9) - 12) %
h -1 ; 13)µg l -1
Table 3 : Extreme values of different parameters obtained from 12 monthly investigations.
Though pool sizes of polymers (including oligomers) and of monomers of the different
substrates investigated are not known, some indication for the mechanism of equilibration between these pools may arise from the comparison of hydrolyzation rate (HR, %
h'
1 ) of the directly available part of the polymer pool and the turnover rate (TR, % h'1 ) of
the corresponding monomer pool. However, one must bear in mind, that the polymer
hydrolyzation rate as measured via MUF-substrates will, at best, provide a relative
measure of that part of the polymer pool which is exposed to enzymatic splitting from the
end points of the macromolecules.
124