scholarly journals The kinetics of inactivation of the rod phototransduction cascade with constant Ca2+i.

1996 ◽  
Vol 107 (1) ◽  
pp. 19-34 ◽  
Author(s):  
A Lyubarsky ◽  
S Nikonov ◽  
E N Pugh
Keyword(s):  
G Protein ◽  
Time Constant ◽  
Inactivation Kinetics ◽  
First Order ◽  
Successful Model ◽  
Ringer’S Solution ◽  
Rhodopsin Kinase ◽  
Solution Bathing ◽  
Kinetics Of ◽  
Phototransduction Cascade

A rich variety of mechanisms govern the inactivation of the rod phototransduction cascade. These include rhodopsin phosphorylation and subsequent binding of arrestin; modulation of rhodopsin kinase by S-modulin (recoverin); regulation of G-protein and phosphodiesterase inactivation by GTPase-activating factors; and modulation of guanylyl cyclase by a high-affinity Ca(2+)-binding protein. The dependence of several of the inactivation mechanisms on Ca2+i makes it difficult to assess the contributions of these mechanisms to the recovery kinetics in situ, where Ca2+i is dynamically modulated during the photoresponse. We recorded the circulating currents of salamander rods, the inner segments of which are held in suction electrodes in Ringer's solution. We characterized the response kinetics to flashes under two conditions: when the outer segments are in Ringer's solution, and when they are in low-Ca2+ choline solutions, which we show clamp Ca2+i very near its resting level. At T = 20-22 degrees C, the recovery phases of responses to saturating flashes producing 10(2.5)-10(4.5) photoisomerizations under both conditions are characterized by a dominant time constant, tau c = 2.4 +/- 0.4 s, the value of which is not dependent on the solution bathing the outer segment and therefore not dependent on Ca2+i. We extended a successful model of activation by incorporating into it a first-order inactivation of R*, and a first-order, simultaneous inactivation of G-protein (G*) and phosphodiesterase (PDE*). We demonstrated that the inactivation kinetics of families of responses obtained with Ca2+i clamped to rest are well characterized by this model, having one of the two inactivation time constants (tau r* or tau PDE*) equal to tau c, and the other time constant equal to 0.4 +/- 0.06 s.

Thermal Inactivation Kinetics of Sporolactobacillus nakayamae Spores, a Spoilage Bacterium Isolated from a Model Mashed Potato–Scallion Mixture

2016 ◽  
Vol 79 (9) ◽  
pp. 1482-1489
Author(s):  
HAYRIYE BOZKURT ◽  
JAIRUS R. D. DAVID ◽  
RYAN J. TALLEY ◽  
D. SCOTT LINEBACK ◽  
P. MICHAEL DAVIDSON
Keyword(s):  
Heat Resistance ◽  
Thermal Inactivation ◽  
Weibull Model ◽  
Inactivation Kinetics ◽  
Order Model ◽  
First Order ◽  
Different Temperatures ◽  
Spoilage Bacterium ◽  
D Values ◽  
Kinetics Of

ABSTRACT Sporolactobacillus species have been occasionally isolated from spoiled foods and environmental sources. Thus, food processors should be aware of their potential presence and characteristics. In this study, the heat resistance and influence of the growth and recovery media on apparent heat resistance of Sporolactobacillus nakayamae spores were studied and described mathematically. For each medium, survivor curves and thermal death curves were generated for different treatment times (0 to 25 min) at different temperatures (70, 75, and 80°C) and Weibull and first-order models were compared. Thermal inactivation data for S. nakayamae spores varied widely depending on the media formulations used, with glucose yeast peptone consistently yielding the highest D-values for the three temperatures tested. For this same medium, the D-values ranged from 25.24 ± 1.57 to 3.45 ± 0.27 min for the first-order model and from 24.18 ± 0.62 to 3.50 ± 0.24 min for the Weibull model at 70 and 80°C, respectively. The z-values determined for S. nakayamae spores were 11.91 ± 0.29°C for the Weibull model and 11.58 ± 0.43°C for the first-order model. The calculated activation energy was 200.5 ± 7.3 kJ/mol for the first-order model and 192.8 ± 22.1 kJ/mol for the Weibull model. The Weibull model consistently produced the best fit for all the survival curves. This study provides novel and precise information on thermal inactivation kinetics of S. nakayamae spores that will enable reliable thermal process calculations for eliminating this spoilage bacterium.

scholarly journals Thermal Inactivation Kinetics of Human Norovirus Surrogates and Hepatitis A Virus in Turkey Deli Meat

2015 ◽  
Vol 81 (14) ◽  
pp. 4850-4859 ◽  
Author(s):  
Hayriye Bozkurt ◽  
Doris H. D'Souza ◽  
P. Michael Davidson
Keyword(s):  
Hepatitis A ◽  
Thermal Inactivation ◽  
Hepatitis A Virus ◽  
Weibull Model ◽  
Activation Energies ◽  
Inactivation Kinetics ◽  
Order Model ◽  
Decimal Reduction Time ◽  
First Order ◽  
Kinetics Of

ABSTRACTHuman noroviruses (HNoV) and hepatitis A virus (HAV) have been implicated in outbreaks linked to the consumption of presliced ready-to-eat deli meats. The objectives of this research were to determine the thermal inactivation kinetics of HNoV surrogates (murine norovirus 1 [MNV-1] and feline calicivirus strain F9 [FCV-F9]) and HAV in turkey deli meat, compare first-order and Weibull models to describe the data, and calculate Arrhenius activation energy values for each model. TheD(decimal reduction time) values in the temperature range of 50 to 72°C calculated from the first-order model were 0.1 ± 0.0 to 9.9 ± 3.9 min for FCV-F9, 0.2 ± 0.0 to 21.0 ± 0.8 min for MNV-1, and 1.0 ± 0.1 to 42.0 ± 5.6 min for HAV. Using the Weibull model, thetD = 1(time to destroy 1 log) values for FCV-F9, MNV-1, and HAV at the same temperatures ranged from 0.1 ± 0.0 to 11.9 ± 5.1 min, from 0.3 ± 0.1 to 17.8 ± 1.8 min, and from 0.6 ± 0.3 to 25.9 ± 3.7 min, respectively. Thez(thermal resistance) values for FCV-F9, MNV-1, and HAV were 11.3 ± 2.1°C, 11.0 ± 1.6°C, and 13.4 ± 2.6°C, respectively, using the Weibull model. Thezvalues using the first-order model were 11.9 ± 1.0°C, 10.9 ± 1.3°C, and 12.8 ± 1.7°C for FCV-F9, MNV-1, and HAV, respectively. For the Weibull model, estimated activation energies for FCV-F9, MNV-1, and HAV were 214 ± 28, 242 ± 36, and 154 ± 19 kJ/mole, respectively, while the calculated activation energies for the first-order model were 181 ± 16, 196 ± 5, and 167 ± 9 kJ/mole, respectively. Precise information on the thermal inactivation of HNoV surrogates and HAV in turkey deli meat was generated. This provided calculations of parameters for more-reliable thermal processes to inactivate viruses in contaminated presliced ready-to-eat deli meats and thus to reduce the risk of foodborne illness outbreaks.

Inactivation Kinetics of Avirulent Bacillus anthracis Spores in Milk with a Combination of Heat and Hydrogen Peroxide

2008 ◽  
Vol 71 (2) ◽  
pp. 333-338 ◽  
Author(s):  
SA XU ◽  
THEODORE P. LABUZA ◽  
FRANCISCO DIEZ-GONZALEZ
Keyword(s):  
Hydrogen Peroxide ◽  
Bacillus Anthracis ◽  
Capillary Tube ◽  
Inactivation Kinetics ◽  
First Order ◽  
Freeze Dried ◽  
Bacillus Anthracis Spores ◽  
The Mean ◽  
D Values ◽  
Kinetics Of

The combined effect of heat and hydrogen peroxide (HP) on the inactivation of avirulent Bacillus anthracis spores (Sterne strain 7702; strain ANR-1, an avirulent Ames derivative lacking the pXO2 plasmid; and strain 9131, a plasmid-less Sterne strain) was evaluated in milk. The study temperature ranged from 90 to 95°C, and the concentration of added HP varied from 0.05 to 0.5%. Decimal reduction times (D-values) were determined using a sealed capillary tube technique. The mean D- and z-values of hydrated freeze-dried spores of all three strains in milk ranged from 550 s at 90C to180s at 94°C and from 8.6 to 9.0°C, respectively. When 0.05% HP was added to the milk, the D-values were decreased at least threefold, and at 0.5% HP the D-values ranged from 1 to 10 s. At 90°C, all three strains had similar D-values when 0.05% HP was added. Increasing the concentration of HP to 0.5% had a greater reducing effect on the D-value for strain 7702 than on the values for strains ANR-1 and 9131. The rate of inactivation of each strain followed first-order reaction kinetics at each temperature-peroxide combination. Equations in the form of D = Constant × (HP concentration)n had R2 values greater than 0.97 for strains ANR-1 and 7702 and of at least 0.7 for strain 9131. This study suggests that a combination of high temperature (from 90 to 95°C) and HP could be used for inactivation of B. anthracis spores in the event of deliberate contamination of milk such that the contaminated milk could be disposed of safely.

Thermal Inactivation at High Temperatures and Regeneration of Green Asparagus Peroxidase

1996 ◽  
Vol 59 (10) ◽  
pp. 1065-1071 ◽  
Author(s):  
CARMEN RODRIGO ◽  
MIGUEL RODRIGO ◽  
ANDRÉS ALVARRUIZ ◽  
ANA FRÍGOLA
Keyword(s):  
Enzyme Activity ◽  
Peroxidase Activity ◽  
Thermal Inactivation ◽  
Maximum Activity ◽  
Small Samples ◽  
Inactivation Kinetics ◽  
Optimum Conditions ◽  
First Order ◽  
Kinetics Of ◽  
Green Asparagus

A spectrophotometric method was developed for determining the peroxidase activity of green asparagus in small samples. The optimum conditions for the analysis in the cuvette were 45 mM of H2O2 36 mM of guaiacol, and pH 7. The method can be used to determine enzyme activity at up to two decimal reductions. A study was performed of the regeneration and inactivation kinetics of the enzyme when heated between 90 and 125°C. Regenerated asparagus peroxidase reached its maximum activity after being stored 6 days at 25°C. The regenerated enzyme followed first-order inactivation kinetics, showing an Ea = 13.62 kcal/mol and k100°C = 2.07 min−1.

Evaluation of Chlorine for Inactivation of Bioterrorism Agents in Drinking Water

2013 ◽  
Vol 295-298 ◽  
pp. 599-603
Author(s):  
Feng Liu ◽  
Zhong Lin Chen ◽  
Sheng Chang
Keyword(s):  
Drinking Water ◽  
Free Chlorine ◽  
Inactivation Kinetics ◽  
Lag Phase ◽  
Solution Ph ◽  
First Order ◽  
Pseudo First Order ◽  
Ph Range ◽  
Kinetics Of ◽  
Experimental Temperature Range

The object of this paper is to measure the characteristics of the inactivation kinetics of B. subtilis spores-surrogates for B. anthracis spores following the treatment with free chlorine. The results indicated that the inactivation kinetics of B. subtilis spores with free chlorine was characterized by a lag phase followed by a pseudo-first-order rate of inactivation. The magnitude of the lag phase increased and the rate of subsequent inactivation decreased with the decreasing temperature, for the experimental temperature range of 1-30 °C. The same tendency of inactivation kinetics curves was observed for the increasing solution pH, for the experimental pH range of 6-8. The CT concept was proved to be valid for the inactivation kinetics of B. subtilis spores with free chlorine under the conditions investigated. The validity of B. subtilis spores served as conservative surrogates for B. anthracis spore has been finally discussed.

Inactivation and Regeneration Kinetics of Horseradish Peroxidase Heated at High Temperatures

1997 ◽  
Vol 60 (8) ◽  
pp. 961-966 ◽  
Author(s):  
CARMEN RODRIGO ◽  
MIGUEL RODRIGO ◽  
ANDRÉS ALVARRUIZ ◽  
ANA FRÍGOLA
Keyword(s):  
Horseradish Peroxidase ◽  
High Temperatures ◽  
Storage Temperature ◽  
Maximum Activity ◽  
Inactivation Kinetics ◽  
Capillary Tubes ◽  
Absolute Value ◽  
First Order ◽  
The Absolute ◽  
Kinetics Of

The inactivation kinetics of horseradish peroxidase (HRP) heated in capillary tubes in the range 110 to 135°C was studied. Its regeneration kinetics when stored at 4 and 25°C was also considered. As the severity of the treatment increased, the absolute value of the regeneration decreased. The storage temperature of the enzyme did not affect the percentage of maximum activity regenerable, although when this temperature was raised from 4 to 25°C the speed of regeneration increased. Kinetics of HRP inactivation determined after heating and after regeneration were compared. Both forms of the enzyme showed similar behavior with first-order inactivation kinetics, with Ea = 19.5 ± 1.0 kcal/mol and k120°C = 3.7 ± 0.2 min−1, and Ea = 18.8 ± 1.2 kcal/mol and k120°C = 3.7 ± 0.2 min−1, respectively.

scholarly journals Kinetics of Turn-offs of Frog Rod Phototransduction Cascade

2008 ◽  
Vol 132 (5) ◽  
pp. 587-604 ◽  
Author(s):  
Luba A. Astakhova ◽  
Michael L. Firsov ◽  
Victor I. Govardovskii
Keyword(s):  
Time Constant ◽  
Dark Current ◽  
Main Part ◽  
Time Course ◽  
Light Adaptation ◽  
Key Factors ◽  
Time Courses ◽  
Kinetics Of ◽  
Phototransduction Cascade ◽  
Effect Of Light

The time course of the light-induced activity of phototrandsuction effector enzyme cGMP-phosphodiesterase (PDE) is shaped by kinetics of rhodopsin and transducin shut-offs. The two processes are among the key factors that set the speed and sensitivity of the photoresponse and whose regulation contributes to light adaptation. The aim of this study was to determine time courses of flash-induced PDE activity in frog rods that were dark adapted or subjected to nonsaturating steady background illumination. PDE activity was computed from the responses recorded from solitary rods with the suction pipette technique in Ca2+-clamping solution. A flash applied in the dark-adapted state elicits a wave of PDE activity whose rising and decaying phases have characteristic times near 0.5 and 2 seconds, respectively. Nonsaturating steady background shortens both phases roughly to the same extent. The acceleration may exceed fivefold at the backgrounds that suppress ≈70% of the dark current. The time constant of the process that controls the recovery from super-saturating flashes (so-called dominant time constant) is adaptation independent and, hence, cannot be attributed to either of the processes that shape the main part of the PDE wave. We hypothesize that the dominant time constant in frog rods characterizes arrestin binding to rhodopsin partially inactivated by phosphorylation. A mathematical model of the cascade that considers two-stage rhodopsin quenching and transducin inactivation can mimic experimental PDE activity quite well. The effect of light adaptation on the PDE kinetics can be reproduced in the model by concomitant acceleration on both rhodopsin phosphorylation and transducin turn-off, but not by accelerated arrestin binding. This suggests that not only rhodopsin but also transducin shut-off is under adaptation control.

Saccharomyces cerevisiae Thermal Inactivation Kinetics Combined with Ultrasound

1999 ◽  
Vol 62 (10) ◽  
pp. 1215-1217 ◽  
Author(s):  
A. LÓPEZ-MALO ◽  
S. GUERRERO ◽  
S. M. ALZAMORA
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Thermal Inactivation ◽  
Order Reaction ◽  
Heat Inactivation ◽  
Inactivation Kinetics ◽  
Thermal Treatments ◽  
Combined Treatments ◽  
First Order ◽  
D Values ◽  
Kinetics Of

Inactivation kinetics of Saccharomyces cerevisiae during thermal treatments at moderate temperatures (45.0, 47.5, 50.0, 52.5, or 55.0°C) combined with application of 20 kHz of ultrasound were evaluated. S. cerevisiae inactivation under the combined effects of heat and ultrasound followed first-order reaction kinetics, with decimal reduction times (D) that varied from 22.3 to 0.8 min. D values in treatments that combined heat and ultrasound were significantly smaller (P < 0.05) than D values obtained for thermal treatments and were more noticeable at temperatures below 50°C. The dependence of the D value on temperature had a significantly (P < 0.05) greater z value for combined treatments. Yeast heat inactivation kinetics revealed decreased thermal resistance caused by ultrasound.

scholarly journals Kinetics of Inactivation of Bacillus subtilis subsp.nigerSpores and Staphylococcus albus on Paper by Chlorine Dioxide Gas in an Enclosed Space

2016 ◽  
Vol 82 (10) ◽  
pp. 3061-3069 ◽  
Author(s):  
Tao Wang ◽  
Jinhui Wu ◽  
Jiancheng Qi ◽  
Limei Hao ◽  
Ying Yi ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Chlorine Dioxide ◽  
Biological Indicators ◽  
Inactivation Kinetics ◽  
Rapid Improvement ◽  
Content Type ◽  
Gas Concentration ◽  
First Order ◽  
Log Reduction ◽  
Kinetics Of

ABSTRACTBacillus subtilissubsp.nigerspore andStaphylococcus albusare typical biological indicators for the inactivation of airborne pathogens. The present study characterized and compared the behaviors ofB. subtilissubsp.nigerspores andS. albusin regard to inactivation by chlorine dioxide (ClO2) gas under different gas concentrations and relative humidity (RH) conditions. The inactivation kinetics under different ClO2gas concentrations (1 to 5 mg/liter) were determined by first-order and Weibull models. A new model (the Weibull-H model) was established to reveal the inactivation tendency and kinetics for ClO2gas under different RH conditions (30 to 90%). The results showed that both the gas concentration and RH were significantly (P< 0.05) and positively correlated with the inactivation of the two chosen indicators. There was a rapid improvement in the inactivation efficiency under high RH (>70%). Compared with the first-order model, the Weibull and Weibull-H models demonstrated a better fit for the experimental data, indicating nonlinear inactivation behaviors of the vegetative bacteria and spores following exposure to ClO2gas. The times to achieve a six-log reduction ofB. subtilissubsp.nigerspore andS. albuswere calculated based on the established models. Clarifying the kinetics of inactivation ofB. subtilissubsp.nigerspores andS. albusby ClO2gas will allow the development of ClO2gas treatments that provide an effective disinfection method.IMPORTANCEChlorine dioxide (ClO2) gas is a novel and effective fumigation agent with strong oxidization ability and a broad biocidal spectrum. The antimicrobial efficacy of ClO2gas has been evaluated in many previous studies. However, there are presently no published models that can be used to describe the kinetics of inactivation of airborne pathogens by ClO2gas under different gas concentrations and RH conditions. The first-order and Weibull (Weibull-H) models established in this study can characterize and compare the behaviors ofBacillus subtilissubsp.nigerspores andStaphylococcusalbusin regard to inactivation by ClO2gas, determine the kinetics of inactivation of two chosen strains under different conditions of gas concentration and RH, and provide the calculated time to achieve a six-log reduction. These results will be useful to determine effective conditions for ClO2gas to inactivate airborne pathogens in contaminated air and other environments and thus prevent outbreaks of airborne illness.

Determination of the Thermal Inactivation Kinetics of the Human Norovirus Surrogates, Murine Norovirus and Feline Calicivirus

2013 ◽  
Vol 76 (1) ◽  
pp. 79-84 ◽  
Author(s):  
HAYRIYE BOZKURT ◽  
DORIS H. D'SOUZA ◽  
P. MICHAEL DAVIDSON
Keyword(s):  
Thermal Inactivation ◽  
Weibull Model ◽  
Inactivation Kinetics ◽  
Feline Calicivirus ◽  
Murine Norovirus ◽  
Order Model ◽  
Human Norovirus ◽  
First Order ◽  
D Values ◽  
Kinetics Of

Studies are needed to bridge existing data gaps and determine appropriate parameters for thermal inactivation methods for human noroviruses. Cultivable surrogates, such as feline calicivirus (FCV-F9) and murine norovirus (MNV-1), have been used in the absence of human norovirus infectivity assays. This study aimed to characterize the thermal inactivation kinetics of MNV-1 and FCV-F9 at 50, 56, 60, 65, and 72°C for different treatment times (0 to 60 min). Thermal inactivation was performed using the capillary tube method with titers of 4.0 × 107 (MNV-1) and 5.8 × 108 (FCV-F9) PFU/ml in triplicate experiments, followed by standard plaque assays in duplicate for each experiment. Weibull and first-order models were compared to describe survival curve kinetics. Model fitness was investigated by comparing the regression coefficients (R2) and the chi-square (χ2) and root mean square error (RMSE) values. The D-values calculated from the first-order model (50 to 72°C) were 0.15 to 34.49 min for MNV-1 and 0.11 to 20.23 min for FCV-9. Using the Weibull model, the tD values needed to destroy 1 log PFU of MNV-1 and FCV-F9 at the same temperatures were 0.11 to 28.26 and 0.06 to 13.86 min, respectively. In terms of thermal resistance, MNV-1 was more sensitive than FCV-F9 up to 65°C. At 72°C, FCV-F9 was slightly more susceptible to heat inactivation. Results revealed that the Weibull model was more appropriate to represent the thermal inactivation behavior of both tested surrogates. The z-values were calculated using D-values for the first-order model and the tD values for the Weibull model. The z-values were 9.31 and 9.19°C for MNV-1 and 9.36 and 9.31°C for FCV-F9 for the first-order and Weibull models, respectively. This study provides more precise information than previous reports on the thermal inactivation kinetics of two norovirus surrogates for use in thermal process calculations.

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