Thermal and pH stability of pestiviruses.
نویسندگان
چکیده
Three strains/isolates of hog cholera virus (HCV) and two strains/isolates each of cytopathogenic (cp) and non-cytopathogenic (ncp) biotype of bovine virus diarrhoea virus (BVDV) were each exposed to pH 3, 3.5 and 4 at 4 degrees C, 21 degrees C and 37 degrees C in a number of combinations. Infectivity titration and half-life determinations following correlation and regression analysis showed a significant temperature-dependent shortening of half-lives within the pH range investigated. At pH 3, mean half-lives were more than tenfold lower when HCV was kept at an ambient temperature of 21 degrees C rather than at 4 degrees C. Additionally, in some of the strains/isolates tested, half-lives of HCV kept at 4 degrees C were four to ten times lower when the pH was raised from 3 to 4. BVDV appeared more sensitive at 4 degrees C and pH 3 than HCV, but equally sensitive at 21 degrees C. Differences in temperature or pH stability between cp and ncp biotypes of BVDV could not be statistically verified although, in general, the cp biotypes seemed to be more stable than the ncp strains/isolates.
منابع مشابه
Preparation of CuO/Water Nanofluids Using Polyvinylpyrolidone and a Survey on Its Stability and Thermal Conductivity
In this article CuO/water nanofluid was synthesized by using polyvinylpyrolidone (PVP) as the dispersant. Thenanofluid stability period and the heat transfer enhancement were determinedby measuring the thermal conductivities. To study the nano-fluid stability, zeta (ζ) potential, and absorbency were measured under different pH values and PVP surfactant concentrations; also thermal conductivity...
متن کاملA Comparative Study of Activity and Stability of the Free and the Immobilized Endoglucanase from Alicyclobacillus Acidocaldarius
AaCel9A [β-1,4-endoglucanase, (E.C:3.2.1.4)], was immobilized onto glutaraldehyde activated chitosan macrosphere by covalent attachment. The properties of the immobilized AaCel9A were investigated by determining the optimum pH and optimum temperature for activity, thermal stability, and kinetic parameters. The immobilization process shifted the enzyme’s optimum temperature from 65 °C for the fr...
متن کاملThermal stability of a-Lactalbumin in the presence of various sugars as osmolytes
Thermal denaturation of a-Lactalbumin in the absence and presence of various concentrations of sucrose,sorbitol, glucose and galactose as sugar osmolytes were measured by monitoring changes in the absorptions thatcarried out in a Lambd 35 UV-Vis double beam spectrophotometer at pH 6.0. These measurements gave valuesof T., (midpoint of denaturation), AH., (enthalpy change at T.), and ACp (consta...
متن کاملThermal stability of P-lactoglobulin Bin the presence of ‘ucrnse, sorbitol and trehalose as osmolJtes
Thermal denaturation of p-Iactoglobulin type B in the absence and pteNcno: of g arious concentrations oftrehalo5e, sucrose and sork toles sugar osmolytes and twlyols were nuyoured hy monitoring changes in theabsorption coefficients at pH 2.0. These measurements gave aliss, or I. mpdpDint of denaturation), Al-fis(enthalpy change at Ty). and ACp (consttun-pressure heal capaciit eh.iltgtii under a...
متن کاملThe Effect of TiO2-Nanoparticle on the Activity and Stability of Trypsin in Aqueous Medium
Trypsin (E.C.3.4.21.4) is a serine protease commonly used in proteomics for digestion of proteins. In the present study, the effect of nano-TiO2 on the conformation and catalytic activity of trypsin were studied. The thermal denaturation of trypsin has been investigated in the presence and absence of nano-TiO2 over the temperature range (293-373 K) at pH 3.0 and 7.25, using temperature scanning...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Revue scientifique et technique
دوره 11 3 شماره
صفحات -
تاریخ انتشار 1992