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1.
Mar Pollut Bull ; 195: 115424, 2023 Oct.
Article in English | MEDLINE | ID: mdl-37659383

ABSTRACT

This research deals with the land-based pressures on the southern Black Sea coast (Turkey), with the objective of assessing their eutrophication impacts. In this context, reference values of some of the eutrophication indicators were calculated, and eutrophication assessment was carried out for this area using the holistic approach NEAT (Nested Environmental Status Assessment Tool). In addition, correlations between NEAT results of coastal regions and pressure-impact analysis methods were investigated. In the determined Spatial Assessment Unit (SAU) areas, 9 indicators were evaluated according to the SAU surface, both with and without weighting by their size the overall assessment of the Turkish Black Sea coast is good (0.70) and moderate (0.57) environmental status, for non-weighting and weighting by SAUs, respectively, with a high confidence level. With this study, we concluded that the sensitivity of the assessment tool needs to be increased. Despite these results, an appropriate number of indicators to represent the water column should be added. It is important to include the phytoplankton variable in the evaluation in future studies. In addition, this study, which uses NEAT allows identifying problematic environmental areas that require attention and action from managers and policymakers.

2.
Talanta ; 79(5): 1412-7, 2009 Oct 15.
Article in English | MEDLINE | ID: mdl-19635378

ABSTRACT

The gene for Clostridium thermocellum L-lactate dehydrogenase enzyme was cloned into pGEX-4T-2 purification vector to supply a source for a thermostable enzyme in order to produce a stable lactate biosensor working at relatively high temperatures. The purified thermostable enzyme (t-LDH) was then immobilized on a gold electrode via polymerization of polygluteraldehyde and pyrrol resulting in a conductive co-polymer. t-LDH working electrode (t-LDHE) was used for determination of lactate in CHES buffer. Amperometric response of the produced electrodes was measured as a function of lactate concentration, at a fixed bias voltage of 200 mV in a three-electrode system. The linear range and sensitivity of the biosensor was investigated at various temperatures in the range of 25-60 degrees C. The sensitivity t-LDHE increased with increasing the temperature and reached its highest value at 60 degrees C. The calculated value was nearly 70 times higher as compared to the sensitivity value of the same electrode tested at 25 degrees C. The sensing parameters of t-LDHE were compared with the electrodes produced by commercially available rabbit muscle LDH (m-LDH). The sensitivity of t-LDHE was nearly 8 times higher than that of m-LDHE. t-LDHE was found to retain its activity for a week incubation at refrigerator (+5 degrees C), while m-LDHE lost its activity in this period. t-LDHE was also tested in the presence of human blood serum. The results showed that the current increased with increasing concentrations of lactate in the human blood serum and the biosensor is more sensitive to serum lactate as well as the commercial lactate dissolved in serum as compared to the commercial lactate dissolved in CHES buffer.


Subject(s)
Biosensing Techniques/methods , L-Lactate Dehydrogenase , Lactic Acid/blood , Animals , Clostridium thermocellum/enzymology , Electrochemical Techniques , Enzyme Stability , Enzymes, Immobilized , Hot Temperature , Humans , Rabbits , Temperature
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