Effect of pH and temperature on alcohol dehydrogenase

1979 ◽  
Vol 44 (3) ◽  
pp. 986-990 ◽  
Author(s):  
Sylva Leblová ◽  
Roman Lapka ◽  
Noemi Nováková

Alcohol dehydrogenase isolated from germinating pea seeds catalyzes ethanol oxidation at pH 8.7 and acetaldehyde reduction at pH 7.0. The values of the Michaelis constants are the lowest in the range of pH-optimums. The effect of temperature on the reaction rate was investigated over the range 15-55 °C. The initial and maximal rates increase with the increasing temperature and attain a maximum at 40 °C. The values of the Michaelis constants are the lowest at 21 °C. Pea alcohol dehydrogenase looses its activity at 70 °C, the binary enzyme-NAD complex is more thermostable.

2018 ◽  
Vol 15 (2) ◽  
pp. 158-168
Author(s):  
Baghdad Science Journal

In this research, the degradation of Dazomet has been studied by using thermal Fenton process and photo-Fenton processes under UV and lights sun. The optimum values of amounts of the Fenton reagents have been determined (0.07g FeSO4 .7H2O, 3.5µl H2O2) at 25 °C and at pH 7 where the degradation percentages of Dazomet were recorded high. It has been found that solar photo Fenton process was more effective in degradation of Dazomet than photo-Fenton under UV-light and thermal Fenton processes, the percentage of degradation of Dazomet by photo-Fenton under sun light are 88% and 100% at 249 nm and 281 nm respectively, while the percentages of degradation for photo-Fenton under UV-light are 87%, 96% and for thermal Fenton are 70% and 66.8% at 249 nm and 281 nm respectively. In this research the effect of temperature on all the reactions has been studied in the range 25°C-45°C, it has been noticed that the reaction rate constant (k) has increased with increasing temperature, and the best percentage degradation of Dazomet was at 45°C in all processes, so, the thermodynamic functions ?G*, ?H*, ?S* have been calculated


1966 ◽  
Vol 49 (5) ◽  
pp. 989-1005 ◽  
Author(s):  
Richard Fitzhugh

In the squid giant axon, Sjodin and Mullins (1958), using 1 msec duration pulses, found a decrease of threshold with increasing temperature, while Guttman (1962), using 100 msec pulses, found an increase. Both results are qualitatively predicted by the Hodgkin-Huxley model. The threshold vs. temperature curve varies so much with the assumptions made regarding the temperature-dependence of the membrane ionic conductances that quantitative comparison between theory and experiment is not yet possible. For very short pulses, increasing temperature has two effects. (1) At lower temperatures the decrease of relaxation time of Na activation (m) relative to the electrical (RC) relaxation time favors excitation and decreases threshold. (2) For higher temperatures, effect (1) saturates, but the decreasing relaxation times of Na inactivation (h) and K activation (n) factor accommodation and increased threshold. The result is a U-shaped threshold temperature curve. R. Guttman has obtained such U-shaped curves for 50 µsec pulses. Assuming higher ionic conductances decreases the electrical relaxation time and shifts the curve to the right along the temperature axis. Making the conductances increase with temperature flattens the curve. Using very long pulses favors effect (2) over (1) and makes threshold increase monotonically with temperature.


Author(s):  
Siqi Tang ◽  
Seungrag Choi ◽  
Lawrence Tavlarides

To understand the effect of temperature to the adsorption, 104 ppbv and 1044 ppbv methyl iodide (CHI) adsorptions on reduced silver-functionalized silica aerogel (Ag-Aerogel) at 100, 150 and 200 ℃ were performed. In the experiments, a significantly high uptake rate (3 – 4 times higher than that at 100 and 150 ℃) was observed for the 104 ppbv adsorption at 200 ℃. To explain such behavior, a potential reaction pathway was proposed and multiple physical analyses including nitrogen titration, x-ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM) were performed. Based on the results, the contributing factors appear to be the formation of different Ag-I components induced by temperature, higher silver site availability, decreasing diffusion limitation, and increasing reaction rate described by the Arrhenius relationship.


Author(s):  
Shuo Xu ◽  
Shi-Jie Wang ◽  
Li Xiao-Hong ◽  
Hong-Ling Cui

Defect and doping are effective methods to modulate the physical and chemical properties of materials. In this report, we investigated the structural stability, electronic properties and quantum capacitance (Cdiff) of Zr2CO2 by changing the dopants of Si, Ge, Sn, N, B, S and F in the substitutional site. The doping of F, N, and S atoms makes the system undergo the semiconductor-to-conductor transition, while the doping of Si, Ge, and Sn maintains the semiconductor characteristics. The Cdiff of the doped systems are further explored. The B-doped system can be used as cathode materials, while the systems doped by S, F, N, Sn atoms are promising anode materials of asymmetric supercapacitors, especially for the S-doped system. The improved Cdiff mainly originates from Fermi-level shifts and Fermi-Dirac distribution by the introduction of the dopant. The effect of temperature on Cdiff is further explored. The result indicates that the maximum Cdiff of the studied systems gradually decreases with the increasing temperature. Our investigation can provide useful theoretical basis for designing and developing the ideal electrode materials for supercapacitors.


2021 ◽  
Vol 12 (6) ◽  
pp. 7239-7248

The novel coronavirus, recognized as COVID-19, is the cause of an infection outbreak in December 2019. The effect of temperature and pH changes on the main protease of SARS-CoV-2 were investigated using all-atom molecular dynamics simulation. The obtained results from the root mean square deviation (RMSD) and root mean square fluctuations (RMSF) analyses showed that at a constant temperature of 25℃ and pH=5, the conformational change of the main protease is more significant than that of pH=6 and 7. Also, by increasing temperature from 25℃ to 55℃ at constant pH=7, a remarkable change in protein structure was observed. The radial probability of water molecules around the main protease was decreased by increasing temperature and decreasing pH. The weakening of the binding energy between the main protease and water molecules due to the increasing temperature and decreasing pH has reduced the number of hydrogen bonds between the main protease and water molecules. Finding conditions that alter the conformation of the main protease could be fundamental because this change could affect the virus’s functionality and its ability to impose illness.


1972 ◽  
Vol 130 (3) ◽  
pp. 797-803 ◽  
Author(s):  
C. Brownson ◽  
N. Spencer

1. The partial purification of adenylate kinase, types 1 and 2, from human erythrocytes is described. 2. Gel chromatography of both forms of the enzyme gave estimates of the molecular weights in the range 20000–23000. 3. Studies on crude haemolysates at various pH values indicated that the type 2 enzyme was less stable than the type 1. Heat denaturation studies on the partially purified enzymes confirmed these findings. 4. Measurements of rates of inhibition by iodoacetate and iodoacetamide showed that the type 2 enzyme reacts more readily than the type 1 enzyme with both reagents. 5. The effect of temperature on the initial velocity of ADP formation was measured at a single concentration of both AMP and MgATP2-. The two forms of the enzyme responded differently to increasing temperature.


1978 ◽  
Vol 31 (1) ◽  
pp. 97-101 ◽  
Author(s):  
Maria A. Gionfriddo ◽  
Charles L. Vigue

SUMMARYD. melanogaster imagoes were collected weekly throughout the summer and early fall of 1976. Their Adh genotypes were determined by electrophoresis. The frequency of the Adh4 isoallele fluctuated throughout the period of study. Correlation coefficients assuming no delay, one week delay, two weeks' delay, three weeks' delay, and a four-week delay of the effect of temperature on the frequency of the Adh4 isoallele were insignificant. It was concluded that temperature alone may not be a selective factor but may be selective in combination with other environmental factors.


2000 ◽  
Vol 67 (3) ◽  
pp. 403-413 ◽  
Author(s):  
RICHARD IPSEN ◽  
JEANETTE OTTE ◽  
STIG B. LOMHOLT ◽  
KARSTEN B. QVIST

Whey protein isolate (WPI), either untreated or pretreated at 80 °C for 30 min, was incubated with a proteinase from Bacillus licheniformis until a gel was formed. Standardized reaction times, directly linked to the degree of hydrolysis, were obtained from plots of the relative amount of peptides released v. reaction time obtained under different conditions (enzyme concentration, temperature, pH, NaCl addition). This provided a connection between the gelation profile and the degree of hydrolysis. In the case of untreated WPI, gelation occurred at lower degrees of proteolysis when the enzyme concentration was decreased, demonstrating that a rate-limiting aggregation process occurred at the same time as the proteolysis in a manner similar to the renneting of milk. This was not the case for preheated WPI, when gelation was found to take place at a constant degree of proteolysis, independent of the enzyme concentration. In this case, the mechanism could be described by assuming the thermally induced aggregates present in this substrate had progressively more stabilizing peptide segments shaved off, resulting in increased attraction between individual aggregates that ultimately led to gelation. Results obtained at 40–60 °C supported this, as we found no effect of temperature on the degree of proteolysis at gelation for the untreated WPI, whereas the degree of proteolysis decreased with increasing temperature when heated WPI was hydrolysed. The effect of pH and NaCl addition on the process was to reduce repulsion between the aggregating species so that gelation was induced at a decreased degree of proteolysis.


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