FN Archimer Export Format PT J TI Spatial patterns of ectoenzymatic kinetics in relation to biogeochemical properties in the Mediterranean Sea and the concentration of the fluorogenic substrate used BT AF Van Wambeke, France Pulido, Elvira Catala, Philippe Dinasquet, Julie Djaoudi, Kahina Engel, Anja Garel, Marc Guasco, Sophie Barbara, Marie Nunige, Sandra Taillandier, Vincent Zancker, Birthe Tamburini, Christian AS 1:1;2:1;3:3;4:2,3;5:1,4;6:5;7:1;8:1;9:3;10:1;11:6;12:6,7;13:1; FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:;11:;12:;13:; C1 Aix-Marseille Université, CNRS/INSU, Université de Toulon, IRD, Mediterranean Institute of Oceanography (MIO) UM 110, 13288, Marseille, France Marine Biology Research Division, Scripps Institution of Oceanography, UCSD, La Jolla, USA Sorbonne Universités, UPMC University Paris 6, Laboratoire d'Océanographie Microbienne (LOMIC), Observatoire Océanologique, 66650, Banyuls/mer, France Molecular and Cellular Biology, The University of Arizona, Tucson, USA GEOMAR – Helmholtz-Centre for Ocean Research, Kiel, Germany CNRS, Sorbonne Universités, Laboratoire d’Océanographie de Villefranche (LOV), UMR7093, 06230 Villefranche sur-Mer, France The Marine Biological Association of the UK, Plymouth, United Kingdom C2 UNIV AIX MARSEILLE, FRANCE UNIV CALIF SAN DIEGO, USA UNIV PARIS 6, FRANCE UNIV ARIZONA, USA IFM GEOMAR, GERMANY CNRS, FRANCE MBA, UK IN DOAJ IF 5.092 TC 7 UR https://archimer.ifremer.fr/doc/00642/75452/76268.pdf https://archimer.ifremer.fr/doc/00642/75452/76269.pdf https://archimer.ifremer.fr/doc/00642/75452/83086.pdf https://archimer.ifremer.fr/doc/00642/75452/83088.pdf LA English DT Article CR PEACETIME BO Pourquoi pas ? AB Ectoenzymatic activity, prokaryotic heterotrophic abundances and production were determined in the Mediterranean Sea. Sampling was carried out in the sub-surface, the deep chlorophyll maximum layer (DCM), the core of the Levantine intermediate waters and in the deeper part of the mesopelagic layers. Michaelis–Menten kinetics were assessed using a large range of concentrations of fluorogenic substrates (0.025 to 50 µM). As a consequence, Km (Michaelis–Menten half-saturation constant) and Vm (maximum hydrolysis velocity) parameters were determined for both low- and high-affinity enzymes for alkaline phosphatase, aminopeptidase (LAP) and β-glucosidase (βGLU). Based on the constant derived from the high-LAP-affinity enzyme (0.025–1 µM substrate concentration range), in situ hydrolysis of N proteins contributed 48 % ± 30 % to the heterotrophic bacterial nitrogen demand within the epipelagic layers and 180 % ± 154 % in the Levantine intermediate waters and the upper part of the mesopelagic layers. The LAP hydrolysis rate was higher than bacterial N demand only within the deeper layer and only when considering the high-affinity enzyme. Based on a 10 % bacterial growth efficiency, the cumulative hydrolysis rates of C proteins and C polysaccharides contributed on average 2.5 % ± 1.3  % to the heterotrophic bacterial carbon demand in the epipelagic layers sampled (sub-surface and DCM). This study clearly reveals potential biases in current and past interpretations of the kinetic parameters for the three enzymes tested based on the fluorogenic-substrate concentration used. In particular, the LAP / βGLU enzymatic ratios and some of the depth-related trends differed between the use of high and low concentrations of fluorogenic substrates. PY 2021 PD APR SO Biogeosciences SN 1726-4170 PU Copernicus GmbH VL 18 IS 7 UT 000639027200001 BP 2301 EP 2323 DI 10.5194/bg-18-2301-2021 ID 75452 ER EF