Thermal stability of myosin and protective effect of F-actin on myosin affect the thermal inactivation of calcium-ATPase in unstable kuruma prawn myofibrils

2019 ◽  
Vol 85 (4) ◽  
pp. 757-765
Author(s):  
Takayuki Sasaki ◽  
Masahito Matsukawa
Keyword(s):  
Thermal Stability ◽  
Protective Effect ◽  
Thermal Inactivation ◽  
Calcium Atpase ◽  
Thermal Stability Of

scholarly journals Further thermal characterization of an aspartate aminotransferase from a halophilic organism

1994 ◽  
Vol 298 (2) ◽  
pp. 465-470 ◽  
Author(s):  
F J G Muriana ◽  
M C Alvarez-Ossorio ◽  
A M Relimpio
Keyword(s):  
Thermal Stability ◽  
Aspartate Aminotransferase ◽  
Thermal Inactivation ◽  
Hydrophobic Interactions ◽  
Thermal Characterization ◽  
Haloferax Mediterranei ◽  
First Order Kinetics ◽  
Effects Of Temperature ◽  
Thermal Stability Of

Aspartate aminotransferase (AspAT, EC 2.6.1.1) from the halophilic archaebacterium Haloferax mediterranei was purified [Muriana, Alvarez-Ossorio and Relimpio (1991) Biochem. J. 278, 149-154] and further characterization of the effects of temperature on the activity and stability of the halophilic AspAT were carried out. The halophilic transaminase is most active at 65 degrees C and stable at high temperatures, under physiological or nearly physiological conditions (3.5 M KCl, pH 7.8). Thermal inactivation (60-85 degrees C) of the halophilic AspAT followed first-order kinetics, 2-oxoglutarate causing a shift of the thermal inactivation curves to higher temperatures. The salt concentration affected the thermal stability of the halophilic transaminase at 60 degrees C, suggesting that disruption of hydrophobic interactions may play an important role in the decreased thermal stability of the enzyme.

scholarly journals Protective effect of vitamin E supplementation on increased thermal stability of collagen in diabetic rats

Diabetologia ◽  
1992 ◽  
Vol 35 (10) ◽  
pp. 913-916 ◽  
Author(s):  
Y. Aoki ◽  
Y. Yanagisawa ◽  
K. Yazaki ◽  
H. Oguchi ◽  
K. Kiyosawa ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Vitamin E ◽  
Protective Effect ◽  
Diabetic Rats ◽  
Thermal Stability Of ◽  
Vitamin E Supplementation

scholarly journals Vaccine Quality Is a Key Factor to Determine Thermal Stability of Commercial Newcastle Disease (ND)Vaccines

Vaccines ◽  
2021 ◽  
Vol 9 (4) ◽  
pp. 363
Author(s):  
Nabila Osman ◽  
Danny Goovaerts ◽  
Serageldeen Sultan ◽  
Jeremy Salt ◽  
Christian Grund
Keyword(s):  
Thermal Stability ◽  
Newcastle Disease ◽  
Thermal Inactivation ◽  
Elevated Temperatures ◽  
Cold Chain ◽  
Climate Conditions ◽  
Vaccine Preparation ◽  
Virus Dose ◽  
Specific Factors ◽  
Thermal Stability Of

Vaccination against Newcastle disease (ND), a devastating viral disease of chickens, is often hampered by thermal inactivation of the live vaccines, in particular in tropical and hot climate conditions. In the past, “thermostable” vaccine strains (I-2) were proposed to overcome this problem but previous comparative studies did not include formulation-specific factors of commercial vaccines. In the current study, we aimed to verify the superior thermal stability of commercially formulated I-2 strains by comparing six commercially available ND vaccines. Subjected to 37 °C as lyophilized preparations, two vaccines containing I-2 strains were more sensitive to inactivation than a third I-2 vaccine or compared to three other vaccines based on different ND strains. However, reconstitution strains proved to have a comparable tenacity. Interestingly, all vaccines still retained a sufficient virus dose for protection (106 EID50) after 1 day at 37 °C. These results suggest that there are specific factors that influence thermal stability beyond the strain-specific characteristics. Exposing ND vaccines to elevated temperatures of 51 and 61 °C demonstrated that inactivation of all dissolved vaccines including I-2 vaccine strains occurred within 2 to 4 h. The results revealed important differences among the vaccines and emphasize the importance of the quality of a certain vaccine preparation rather than the strain it contains. These data highlight that regardless of the ND strain used for vaccine preparation, the appropriate cold chain is mandatory for keeping live ND vaccines efficiency in hot climates.

scholarly journals Immobilization of Soybean Lipoxygenase on Nanoporous Rice Husk Silica by Adsorption: Retention of Enzyme Function and Catalytic Potential

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 291
Author(s):  
Putheary Ngin ◽  
Kyoungwon Cho ◽  
Oksoo Han
Keyword(s):  
Thermal Stability ◽  
Rice Husk ◽  
Thermal Inactivation ◽  
Specific Activity ◽  
Silica Particles ◽  
Soybean Lipoxygenase ◽  
Desorption Kinetics ◽  
Rice Husk Silica ◽  
Kinetics Of ◽  
Thermal Stability Of

Soybean lipoxygenase was immobilized on nanoporous rice husk silica particles by adsorption, and enzymatic parameters of the immobilized protein, including the efficiency of substrate binding and catalysis, kinetic and operational stability, and the kinetics of thermal inactivation, were investigated. The maximal adsorption efficiency of soybean lipoxygenase to the silica particles was 50%. The desorption kinetics of soybean lipoxygenase from the silica particles indicate that the silica-immobilized enzyme is more stable in an anionic buffer (sodium phosphate, pH 7.2) than in a cationic buffer (Tris-HCl, pH 7.2). The specific activity of immobilized lipoxygenase was 73% of the specific activity of soluble soybean lipoxygenase at a high concentration of substrate. The catalytic efficiency (kcat/Km) and the Michaelis–Menten constant (Km) of immobilized lipoxygenase were 21% and 49% of kcat/Km and Km of soluble soybean lipoxygenase, respectively, at a low concentration of substrate. The immobilized soybean lipoxygenase was relatively stable, as the enzyme specific activity was >90% of the initial activity after four assay cycles. The thermal stability of the immobilized lipoxygenase was higher than the thermal stability of soluble lipoxygenase, demonstrating 70% and 45% of its optimal specific activity, respectively, after incubation for 30 min at 45 °C. These results demonstrate that adsorption on nanoporous rice husk silica is a simple and rapid method for protein immobilization, and that adsorption may be a useful and facile method for the immobilization of many biologically important proteins of interest.

An unusual effect of NADP+ on the thermostability of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans

2013 ◽  
Vol 91 (5) ◽  
pp. 295-302 ◽  
Author(s):  
Denis Arutyunov ◽  
Elena Schmalhausen ◽  
Victor Orlov ◽  
Sophie Rahuel-Clermont ◽  
Natalia Nagradova ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Streptococcus Mutans ◽  
Thermal Denaturation ◽  
Thermal Inactivation ◽  
Protein Molecule ◽  
Single Amino Acid ◽  
Binary Complex ◽  
Scanning Calorimetry ◽  
Active Centre ◽  
Thermal Stability Of

Adiabatic differential scanning calorimetry was used to investigate the effect of NADP+ on the irreversible thermal denaturation of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Streptococcus mutans. The GAPN–NADP+ binary complex showed a strongly decreased thermal stability, with a difference of about 20 °C between the temperatures of the thermal transition peak maxima of the complex and the free protein. This finding was similar to the previously described thermal destabilization of GAPN upon binding of inorganic phosphate to the substrate binding site and can be interpreted as the shift of the equilibrium between 2 conformers of tetrameric GAPN upon addition of the coenzyme. Single amino acid substitution, known to abolish the NADP+ binding, cancelled the calorimetric effect of the coenzyme. GAPN thermal inactivation was considerably decelerated in the presence of NADP+ showing that the apparent change in stability of the active centre can be the opposite to that of the whole protein molecule. NADP+ could also reactivate the inactive GAPN* species, obtained by the heating of the apoenzyme below the thermal denaturation transition temperature. These effects may reflect a mechanism that provides GAPN the sufficient flexibility for the earlier observed profound active site reorganizations required during the catalytic cycle. The elevated thermal stability of the apoenzyme may, in turn, be important for maintaining a constant level of active GAPN — an enzyme that is known to be crucial for the effective supply of the reducing equivalents in S. mutans and its ability to grow under aerobic conditions.

scholarly journals Structural features responsible for kinetic thermal stability of a carboxypeptidase from the archaebacterium Sulfolobus solfataricus

1993 ◽  
Vol 295 (3) ◽  
pp. 827-831 ◽  
Author(s):  
A Villa ◽  
L Zecca ◽  
P Fusi ◽  
S Colombo ◽  
G Tedeschi ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Thermal Inactivation ◽  
Metal Removal ◽  
Hydrophobic Interactions ◽  
Sulfolobus Solfataricus ◽  
Structural Features ◽  
Inactivation Rate ◽  
Salt Bridges ◽  
Native Conformation ◽  
Thermal Stability Of

Investigations were performed on the structural features responsible for kinetic thermal stability of a thermostable carboxypeptidase from the thermoacidophilic archaebacterium Sulfolobus solfataricus which had been purified previously and identified as a zinc metalloprotease [Colombo, D'Auria, Fusi, Zecca, Raia and Tortora (1992) Eur. J. Biochem. 206, 349-357]. Removal of Zn2+ by dialysis led to reversible activity loss, which was promptly restored by addition of 80 microM ZnCl2 to the assay mixture. For the first-order irreversible thermal inactivation the metal-depleted enzyme showed an activation energy value of 205.6 kJ.mol-1, which is considerably lower than that of the holoenzyme (494.4 kJ.mol-1). The values of activation free energies, enthalpies and entropies also dropped with metal removal. Thermal inactivation of the apoenzyme was very quick at 80 degrees C, whereas the holoenzyme was stable at the same temperature. These findings suggest a major stabilizing role for the bivalent cation. Chaotropic salts strongly destabilized the holoenzyme, showing that hydrophobic interactions are involved in maintaining the native conformation of the enzyme. However, the inactivation rate was also increased by sodium sulphate, acetate and chloride, which are not chaotropes, indicating that one or more salt bridges concur in stabilizing the active enzyme. Furthermore, at the extremes of the pH-stability curve, NaCl did not affect the inactivation rate, confirming the stabilizing role of intramolecular ionic bonds, as a pH-dependent decrease in stability is likely to occur from breaking of salt bridges involved in maintaining the native conformation of the protein.

scholarly journals Vaccine Quality is a Key Factor to Determine Thermal Stability of Commercial Newcastle Disease (ND) Vaccines

2021 ◽  
Author(s):  
Nabila Osman ◽  
Danny Goovaerts ◽  
Sultan Serageldeen ◽  
Christian Grund
Keyword(s):  
Thermal Stability ◽  
Newcastle Disease ◽  
Thermal Inactivation ◽  
Elevated Temperatures ◽  
Viral Disease ◽  
Cold Chain ◽  
Climate Conditions ◽  
Virus Dose ◽  
Different Strains ◽  
Thermal Stability Of

Vaccination against Newcastle disease (ND), a devastating viral disease of chicken, is often hampered by thermal inactivation of the live vaccines, in particular in tropical and hot climate conditions. In the past “thermostable” vaccine strains (I-2) have been proposed to overcome this problem. In the current study, we compared the thermal stability of 6 commercially available ND vaccines. Subjected to 37°C as lyophilized preparation, two vaccines containing I-2 strains were more sensitive to inactivation than a third I-2 vaccine or when compared to three other vaccines based on different strains. However, after reconstitution strains proved to have a comparable tenacity. Interestingly, all vaccines retained a sufficient virus dose for protection (106 EID50) after 1 day at 37°C, still. However, experiments exposing ND-vaccines to elevated temperatures of 51°C and 61°C, clearly demonstrated inactivation of all dissolved vaccines within 2 to 4 hours. The data indicate preparation that specific factors may influence thermal stability rather than strain specific characteristics. Regardless of the ND strain used, the appropriate cold chain is mandatory for live ND-vaccines.

scholarly journals Study of thermal stability of ascospores Aspergillus (Neosartorya) fischeri depending on the concentration of soluble solids in apple juice

2019 ◽  
Vol 81 (3) ◽  
pp. 91-98
Author(s):  
V. V. Kondratenko ◽  
M. V. Trishkaneva ◽  
M. T. Levshenko ◽  
T. A. Pozdnyakova ◽  
A. Y. Kolokolova
Keyword(s):  
Heat Treatment ◽  
Thermal Stability ◽  
Apple Juice ◽  
Thermal Inactivation ◽  
Soluble Solids ◽  
Stability Parameters ◽  
Mold Fungus ◽  
Rate Of Increase ◽  
Thermal Stability Parameters ◽  
Thermal Stability Of

Kinetic studies of the thermal inactivation of test crop spores are necessary to develop optimal heat treatment regimes for fruit juices. The purpose of the work is to study the dynamics of changes in the thermal stability parameters DT and z depending on changes in the soluble solids content in canned fruit products using the example of certain types of apple juice products with a pH of 3.80. The regularity of thermal inactivation of ascospores of the mesophilic mold Aspergillus fischeri in concentrated apple juice (JAC) with a soluble dry matter (RSV) content of 70%, in restored apple juice with RSV – 11.2%, and in restored apple juice with pulp with RSV – 16% was studied. The parameters of thermal stability were determined by the capillary method at temperatures of 80, 85, 90, and 95 °C. It was experimentally established that the heat resistance of A. fischeri spores in clarified apple juice was DT 95 °С = 0.16 min, and the parameter value z = 6.76 °C, in apple juice with pulp parameters: DT 95 °C = 0.24 min, z – 7.12 °C, in YaKS – DT 95 °C = 0.39 min, and z – 7.8 °C. The dynamics of thermal stability parameters D and z of A. fischeri mold fungus spores (test cultures) versus RSV concentration of juice products was established. The research results showed that with an increase in the concentration of RSV, the thermal stability of spores increases exponentially. The rate of increase in thermal stability decreases with increasing concentration of RSV. Since the concentration of RSV affects the rheological properties of the product (viscosity), this leads to a change in the kinetics of heating in products with convection heat transfer. Therefore, an increase in the concentration of RSV should inevitably lead not only to an increase in the thermal stability of spores of microorganisms, but also to a shift in the region of optimal modes of heat treatment of products toward an increase in the thermal load to ensure regulatory requirements for microbiological safety.

Kinetic and Thermodynamic Study of Plantaricin IIA-1A5, a Bacteriocin Produced by Indonesian Probiotic Lactobacillus plantarum IIA-1A5

2020 ◽  
Vol 27 ◽  
Author(s):  
Muhamad Arifin ◽  
Cahyo Budiman ◽  
Kazuhito Fujiyama ◽  
Irma Isnafia Arief
Keyword(s):  
Thermal Stability ◽  
Thermodynamic Parameters ◽  
Lactobacillus Plantarum ◽  
Thermal Inactivation ◽  
Heating Temperature ◽  
Wide Spectrum ◽  
Exchange Chromatography ◽  
K Value ◽  
Thermal Stability Of ◽  
D Value

Background:: Plantaricin IIA-1A5 is a bacteriocin produced by Lactobacillus plantarum IIA-1A5, a locally isolat-ed probiotic from Indonesia. Plantaricin IIA-1A5 exhibits antibacterial activity against wide spectrum of pathogenic bacte-ria, thus promising to be applied in various food products. Nevertheless, thermal stability of this bacteriocin remains to be fully investigated. Objective:: This study aims to determine thermal stability of plantaricin IIA-1A5 through kinetic and thermodynamic param-eters. Method:: To address, plantaricin IIA-1A5 was purified from Lactobacillus plantarum IIA-1A5, which was growth under whey media, using ammonium sulfate precipitation followed by ion-exchange chromatography. Purified plantaricin IIA-IA5 was then subjected to analysis of its bacteriocin activity. The thermal inactivation of bacteriocin from L. plantarum IIA-1A5 was calculated by incubating the bacteriocin at different temperatures ranging from 60-80 °C for 30 to 90 min, which was then used to calculate its kinetic and thermodynamic parameters. Results:: The result showed the inactivation rates (k-value) were ranging from 0.008 to 0.013 min-1. Heat resistance of plantaricin IIA-1A5 (D-value) at constant heating temperature of 60, 65, 70, 75, and 80 °C were 311.6, 305.9, 294.5, 198.9, and 180.2 min, which indicated a faster inactivation at higher temperatures. D-value sensitivity for temperature changes (z-value) was calculated to be 75.76 °C. Further, thermodynamic analysis suggested that plantaricin IIA-1A5 is thermostable, with activation energy (Ea) of 29.02 kJ mol-1. Conclusion:: This result showed that plantaricin IIA-1A5 is considerably more heat-stable than plantaricin members and promises to be applied in food industries where heat treatments are applied. Furthermore, a possible mechanism by which plantaricin IIA-1A5 maintains its stability was also discussed by referring to its thermodynamic parameters.

scholarly journals Interaction of D-600 with the transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase

2000 ◽  
Vol 279 (1) ◽  
pp. C166-C172 ◽  
Author(s):  
Alicia Ortega ◽  
V. M. Becker ◽  
R. Alvarez ◽  
J. R. Lepock ◽  
H. Gonzalez-Serratos
Keyword(s):  
Thermal Stability ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Thermal Denaturation ◽  
Thermal Inactivation ◽  
Channel Blocker ◽  
Transmembrane Domain ◽  
Muscle Cells ◽  
The Stability ◽  
Thermal Stability Of

Experiments were performed to determine whether the organic Ca2+ channel blocker D-600 (gallopamil), which penetrates into muscle cells, affects sarcoplasmic reticulum (SR) Ca2+ uptake by directly inhibiting the light SR Ca2+-ATPase. We have previously shown that at 10 μM, D-600 inhibits LSR ATP-dependent Ca2+ uptake by 50% but has no effect on ATPase activity (21). These data suggest that the SR Ca2+-ATPase might be a potential target for D-600. The ATPase activity of the enzyme is associated with its hydrophilic cytoplasmic domain, whereas Ca2+ binding and translocation are associated with the transmembrane domain (18). In the present experiments, we determined which of the two domains of the ATPase is affected by D-600. Thermal inactivation experiments using the SR Ca2+-ATPase demonstrated that D-600 decreased the thermal stability of Ca2+ transport but had no effect on the stability of ATPase activity. In addition, D-600 at a concentration of 160 μM did not have any leaking effect of Ca2+ on the Ca2+-loaded SR. Thermal denaturation profiles of SR membranes revealed that D-600 interacts directly with the transmembrane domain of the Ca2+-ATPase. No evidence for interaction with the nucleotide domain was obtained. We conclude that the Ca2+ blocker D-600 inhibits the SR Ca2+ pump specifically by interacting with the transmembrane Ca2+-binding domain of the Ca2+-ATPase.

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