Extracellular enzymatic activities in the aquatic ecosystems of the Danube Delta. 2. Alkaline phosphatase activity

2021 ◽  
Vol 26 (1) ◽  
pp. 2269-2274
Author(s):  
IOAN PĂCEŞILĂ ◽  
EMILIA RADU
Keyword(s):  
Alkaline Phosphatase ◽  
Water Column ◽  
Aquatic Ecosystems ◽  
Temporal Dynamics ◽  
Extracellular Enzyme ◽  
Danube Delta ◽  
Phytoplankton Communities ◽  
Extracellular Enzymatic Activities ◽  
Adjacent Channels ◽  
Hydrolysis Of

Phosphorus is one of the most important inorganic nutrients in aquatic ecosystems, the development and functioning of the phytoplankton communities being often correlated with the degree of availability in assimilable forms of this element. Alkaline phosphatase (AP) is an extracellular enzyme with nonspecific activity that catalyses the hydrolysis of a large variety of organic phosphate esters and release orthophosphates. During 2011-2013, AP Activity (APA) was assessed in the water column and sediments of several aquatic ecosystems from Danube Delta: Roșu Lake, Mândra Lake and their adjacent channels – Roșu-Împuțita and Roșu-Puiu. The intensity of APA widely fluctuated, ranging between 230-2578 nmol p-nitrophenol L-1h-1 in the water column and 2104-15631 nmol p-nitrophenol g-1h-1 in sediment. Along the entire period of the study, APA was the most intense in Roșu-Împuțita channel, for both water and sediment samples. Temporal dynamics revealed its highest values in summer for the water column and in autumn for sediment. Statistical analysis showed significant seasonal diferences of the APA dynamics in spring vs. summer and autumn for the water column, and any relevant diferences for sediment.

scholarly journals Chicken Intestinal Alkaline Phosphatase

1960 ◽  
Vol 43 (6) ◽  
pp. 1149-1169 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Alkaline Phosphatase ◽  
Zinc Ions ◽  
Magnesium Ions ◽  
Intestinal Alkaline Phosphatase ◽  
Reversible Inactivation ◽  
Higher Temperature ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Zn Ions ◽  
Denaturation Of Proteins

Purified chicken intestinal alkaline phosphatase is active at pH 8 to 9, but becomes rapidly inactivated with change of pH to 6 or less. Also, a solution of the inactivated enzyme at pH 4.5 rapidly regains its activity at pH 8. In the range of pH 6 to 8 a solution of purified alkaline phosphatase consists of a mixture of active and inactive enzyme in equilibrium with each other. The rate of inactivation at lower pH and of reactivation at higher pH increases with increase in temperature. Also, the activity at equilibrium in the range of pH 6 to 8 increases with temperature so that a solution equilibrated at higher temperature loses part of its activity on cooling, and vice versa, a rise in temperature shifts the equilibrium toward higher activity. The kinetics of inactivation of the enzyme at lower pH and the reactivation at higher pH is that of a unimolecular reaction. The thermodynamic values for the heat and entropy of the reversible inactivation and reactivation of the enzyme are considerably lower than those observed for the reversible denaturation of proteins. The inactivated enzyme at pH 4 to 6 is rapidly reactivated on addition of Zn ions even at pH 4 to 6. However, zinc ions are unable to replace magnesium ions as cocatalysts for the enzymatic hydrolysis of organic phosphates by alkaline phosphatase.

scholarly journals Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture

1972 ◽  
Vol 127 (1) ◽  
pp. 87-96 ◽  
Author(s):  
P. G. Bolton ◽  
A. C. R. Dean
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Continuous Culture ◽  
Activity Profile ◽  
Glucose Effect ◽  
Ph Values ◽  
Nitrophenyl Phosphate ◽  
Wide Range ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

1. Phosphatase synthesis was studied in Klebsiella aerogenes grown in a wide range of continuous-culture systems. 2. Maximum acid phosphatase synthesis was associated with nutrient-limited, particularly carbohydrate-limited, growth at a relatively low rate, glucose-limited cells exhibiting the highest activity. Compared with glucose as the carbon-limiting growth material, other sugars not only altered the activity but also changed the pH–activity profile of the enzyme(s). 3. The affinity of the acid phosphatase in glucose-limited cells towards p-nitrophenyl phosphate (Km 0.25–0.43mm) was similar to that of staphylococcal acid phosphatase but was ten times greater than that of the Escherichia coli enzyme. 4. PO43−-limitation derepressed alkaline phosphatase synthesis but the amounts of activity were largely independent of the carbon source used for growth. 5. The enzymes were further differentiated by the effect of adding inhibitors (F−, PO43−) and sugars to the reaction mixture during the assays. In particular, it was shown that adding glucose, but not other sugars, stimulated the rate of hydrolysis of p-nitrophenyl phosphate by the acid phosphatase in carbohydrate-limited cells at low pH values (<4.6) but inhibited it at high pH values (>4.6). Alkaline phosphatase activity was unaffected. 6. The function of phosphatases in general is discussed and possible mechanisms for the glucose effect are outlined.

scholarly journals Purification and Characterization of 2,6-β-d-Fructan 6-Levanbiohydrolase fromStreptomyces exfoliatus F3-2

2000 ◽  
Vol 66 (1) ◽  
pp. 252-256 ◽  
Author(s):  
Katsuichi Saito ◽  
Kazuya Kondo ◽  
Ichiro Kojima ◽  
Atsushi Yokota ◽  
Fusao Tomita
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Extracellular Enzyme ◽  
Molecular Weights ◽  
Sds Page ◽  
Monomeric Structure ◽  
Ph Range ◽  
Hydrolysis Of

ABSTRACT Streptomyces exfoliatus F3-2 produced an extracellular enzyme that converted levan, a β-2,6-linked fructan, into levanbiose. The enzyme was purified 50-fold from culture supernatant to give a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weights of this enzyme were 54,000 by SDS-PAGE and 60,000 by gel filtration, suggesting the monomeric structure of the enzyme. The isoelectric point of the enzyme was determined to be 4.7. The optimal pH and temperature of the enzyme for levan degradation were pH 5.5 and 60°C, respectively. The enzyme was stable in the pH range 3.5 to 8.0 and also up to 50°C. The enzyme gave levanbiose as a major degradation product from levan in an exo-acting manner. It was also found that this enzyme catalyzed hydrolysis of such fructooligosaccharides as 1-kestose, nystose, and 1-fructosylnystose by liberating fructose. Thus, this enzyme appeared to hydrolyze not only β-2,6-linkage of levan, but also β-2,1-linkage of fructooligosaccharides. From these data, the enzyme from S. exfoliatus F3-2 was identified as a novel 2,6-β-d-fructan 6-levanbiohydrolase (EC 3.2.1.64 ).

scholarly journals Response of <i>Nodularia spumigena</i> to <i>p</i>CO<sub>2</sub> – Part 2: Exudation and extracellular enzyme activities

2013 ◽  
Vol 10 (1) ◽  
pp. 567-582 ◽  
Author(s):  
S. Endres ◽  
J. Unger ◽  
N. Wannicke ◽  
M. Nausch ◽  
M. Voss ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Organic Matter ◽  
Enzyme Activities ◽  
Extracellular Enzymes ◽  
Extracellular Enzyme ◽  
High Pco2 ◽  
Nodularia Spumigena ◽  
Extracellular Enzyme Activities ◽  
Pco2 Treatment ◽  
Co2 Concentrations

Abstract. The filamentous and diazotrophic cyanobacterium Nodularia spumigena plays a major role in the productivity of the Baltic Sea as it forms extensive blooms regularly. Under phosphorus limiting conditions Nodularia spumigena have a high enzyme affinity for dissolved organic phosphorus (DOP) by production and release of alkaline phosphatase. Additionally, they are able to degrade proteinaceous compounds by expressing the extracellular enzyme leucine aminopeptidase. As atmospheric CO2 concentrations are increasing, we expect marine phytoplankton to experience changes in several environmental parameters, including pH, temperature, and nutrient availability. The aim of this study was to investigate the combined effect of CO2-induced changes in seawater carbonate chemistry and of phosphate deficiency on the exudation of organic matter, and its subsequent recycling by extracellular enzymes in a Nodularia spumigena culture. Batch cultures of Nodularia spumigena were grown for 15 days under aeration with low (180 μatm), medium (380 μatm), and high (780 μatm) CO2 concentrations. Obtained pCO2 levels in the treatments were on median 315, 353, and 548 μatm CO2, respectively. Extracellular enzyme activities as well as changes in organic and inorganic compound concentrations were monitored. CO2 treatment–related effects were identified for cyanobacterial growth, which in turn influenced the concentration of mucinous substances and the recycling of organic matter by extracellular enzymes. Biomass production was increased by 56.5% and 90.7% in the medium and high pCO2 treatment, respectively, compared to the low pCO2 treatment. In total, significantly more mucinous substances accumulated in the high pCO2 treatment, reaching 363 μg Xeq L−1 compared to 269 μg Xeq L−1 in the low pCO2 treatment. However, cell-specific rates did not change. After phosphate depletion, the acquisition of P from DOP by alkaline phosphatase was significantly enhanced. Alkaline phosphatase activities were increased by factor 1.64 and 2.25, respectively, in the medium and high compared to the low pCO2 treatment. We hypothesise from our results that Nodularia spumigena can grow faster under elevated pCO2 by enhancing the recycling of organic matter to acquire nutrients.

scholarly journals Summer aspect of phytoplankton communities in some Montenegrin lakes: Are there changes after more than two decades?

2012 ◽  
Vol 64 (2) ◽  
pp. 745-755
Author(s):  
Jelena Rakocevic
Keyword(s):  
Water Quality ◽  
Sustainable Management ◽  
Aquatic Ecosystems ◽  
Phytoplankton Community ◽  
Management Plan ◽  
Phytoplankton Composition ◽  
Qualitative And Quantitative ◽  
Environmental Monitoring System ◽  
Phytoplankton Communities ◽  
Second Period

Qualitative and quantitative phytoplankton compositions of 10 Montenegrin lakes were investigated in the summer of 2007. The obtained results were compared with a previous study-period that was undertaken two decades ago. In the first period, diatoms numerically dominated the phytoplankton community in all studied lakes, while in the second period, the same was observed only in three of the ten lakes; in other studied lakes the relative contributions of green algae, dinoflagellates and/or cyanobacteria increased, while the contribution of diatoms decreased. The shift observed in phytoplankton composition and diversity in some of the studied lakes indicates an increase in the trophic level over the two decades. The sustainable management plan of the aquatic ecosystems in Montenegro should include the establishment of an environmental monitoring system in order to record any alterations that may take place in water quality.

scholarly journals First report on phytoplankton communities of Barishal City, Bangladesh

2020 ◽  
pp. 142-147
Author(s):  
Shaswati Chakraborty ◽  
Dipalok Karmaker ◽  
Subroto Kumar Das ◽  
Riyad Hossen
Keyword(s):  
Aquatic Ecosystems ◽  
Species Number ◽  
Aquatic Environments ◽  
Primary Producers ◽  
First Report ◽  
Biodiversity Indices ◽  
Phytoplankton Communities ◽  
Living Organisms ◽  
The City ◽  
Total Species

Phytoplanktons, also called microalgae, are microscopic photosynthetic living organisms that generally found in aquatic environments. Although they are considered as the most important primary producers and bioindicators of aquatic ecosystems, there was no previous report found for Barishal City about these tiny organisms. Consequently, the present study selected 10 freshwater reservoirs from the city to investigate phytoplankton communities and listed 110 taxa under 4 phyla, 7 classes, 18 orders, 24 families and 49 genera. The distribution of Chlorophytes was abundant relatively in terms of species number (45 taxa) followed by Euglenophytes, Chlorophytes and Cyanophytes in this area. Only Euglenaceae possessed one-third of the total species of this report. Among all stations, the highest number of taxa was recorded from station 2 and according to nine biodiversity indices, the station 2 and 9 showed comparatively good results. All of the recorded taxa were previously mentioned by different authors from Bangladesh.

A Specific Colorimetric 5′-Nucleotidase Assay Utilizing the Berthelot Reaction

1970 ◽  
Vol 16 (5) ◽  
pp. 396-401 ◽  
Author(s):  
Alan Belfield ◽  
Graham Ellis ◽  
David M Goldberg
Keyword(s):  
Alkaline Phosphatase ◽  
Correction Factor ◽  
Nucleotidase Activity ◽  
Color Yield ◽  
Adenylic Acid ◽  
Barbital Buffer ◽  
Hydrolysis Of

Abstract A sensitive calorimetric assay for 5′-nucleotidase activity is described, which requires 40 µl of serum. Adenosine, formed by hydrolysis of 5′-adenylic acid, is deaminated enzymatically and the ammonia determined with the Berthelot reaction. β-Glycerophosphate is added to suppress hydrolysis of 5′-adenylic acid by alkaline phosphatase. The reaction is optimal at pH 7.9 in 0.05M Michaelis' barbital buffer containing 10 mmoles of MgCl2 per liter. In the Berthelot reaction the MgCl2 causes a precipitate, which is removed without decreasing color yield by adding EDTA. Inhibition of the Berthelot reaction by serum and constituents of the reaction mixture is predictable and can be compensated by a correction factor

A Continuous Spectrophotometric Method for Measuring the Activity of Serum Alkaline Phosphatase

1966 ◽  
Vol 12 (2) ◽  
pp. 70-89 ◽  
Author(s):  
George N Bowers ◽  
Robert B McComb
Keyword(s):  
Alkaline Phosphatase ◽  
Standard Deviation ◽  
Sample Size ◽  
Spectrophotometric Method ◽  
Serum Alkaline Phosphatase ◽  
Serum Alkaline Phosphatase Activity ◽  
Factors Affecting ◽  
Nitrophenyl Phosphate ◽  
Relative Standard ◽  
Hydrolysis Of

Abstract A continuous spectrophotometric method for measuring serum alkaline phosphatase activity is described. The effects of temperature, pH, substrate concentration, type and molarity of the buffer, sample size, cofactors, and inhibitors on the enzymatic hydrolysis of p-nitrophenyl phosphate were studied. The optimal conditions for assay of serum alkaline phosphatase at 30° were found to be 0.75 M 2-amino-2-methyl-1-propanol buffer, pH30° 10.15, 4 mmole substrate, and 100 µl. or less sample size. Studies of the factors affecting analytical precision-i.e., control of reaction temperature, of reagent manufacture, and of standardization-are discussed. The precision of this method was 2.3% (relative standard deviation) on 10 within day replicates and 5.0% on day-to-day replicates spread over a 5-week period. The range of activity for 258 apparently healthy adult blood donors was 6-110 mU./ml. (International milliunits per milliliter), with a mean of 49 and a standard deviation of 14.

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