Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4535763 | Deep Sea Research Part I: Oceanographic Research Papers | 2006 | 16 Pages |
Abstract
The activities of two hydrolytic enzymes (leucine aminopeptidase and β glucosidase), belonging to the particle-bound enzymatic fraction, were measured in open-sea surface waters. Samples were collected along a transect crossing the Indian Ocean during the early NW monsoon period (November and December 2001). The latitudinal pattern of the ectoenzymatic activities highlighted a generally increasing trend of glycolysis approaching the equator, with significantly higher β glucosidase activity (0.79-3.00 nmol lâ1 hâ1) within the latitudinal range from 12°N to 16°S. In this area, the surface waters coming from the Indonesian Throughflow and the Bay of Bengal carry a considerable quantity of carbohydrates (38.9-41.9 μg lâ1), which stimulated glycolytic activity and its cell-specific rates scaled to bacterial abundance. On the other hand, in the Central Indian Ocean, the proteolytic activity was considerable (0.91-2.03 nmol lâ1 hâ1), although the particulate proteins did not show significant increases and the dissolved proteinlike signal was one of the lowest of the entire transect (0.7 mg lâ1 on average compared to the 1.4-1.6 mg lâ1 of the adjacent areas). Therefore, in this area, the two ectoenzymes studied did not respond to the same stimulatory effect (namely the specific substrate concentrations). The time needed for the hydrolysis of macromolecules within the particulate and dissolved organic substrate fractions, although these measures are affected by a number of assumptions starting with the potential nature of the ectoenzymatic determinations, confirms these observations. The Central Indian Ocean displayed the lowest values, from 8 to 26 days for particulate and dissolved organic carbon, respectively. As observed in the equatorial areas of the Atlantic Ocean, the relevant degradation activity of the central area of the Indian Ocean Basin suggests a notable heterotrophy based on a faster turnover of organic substrates.
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Authors
C. Misic, M. Castellano, M. Fabiano, N. Ruggieri, V. Saggiomo, P. Povero,