التفاصيل البيبلوغرافية
| العنوان: |
Kinetic Analysis about the Effects of Neutral Salts on the Thermal Stability of Yeast Alcohol Dehydrogenase. |
| المؤلفون: |
Ikegaya, Kazuo |
| المصدر: |
Journal of Biochemistry; Mar2005, Vol. 137 Issue 3, p349-354, 6p |
| مصطلحات موضوعية: |
SALTS, DEHYDROGENASES, YEAST, ENZYMES, BIOCHEMISTRY |
| مستخلص: |
The effects of salts on the rate constants of inactivation by heat of yeast alcohol dehydrogenase (YADH) at 60.0°C were measured. Different effects were observed at low and high salt concentrations. At high concentrations, some salts had stabilizing effects, while others were destabilizing. The effects of salts in the high concentration range examined can be described as follows: (decreased thermal stability) NaClO4 < NaI = (C2H5)4NBr < NH4Br < NaBr = KBr = CsBr = (no addition) < (CH3)4NBr < KCl < KF < Na2SO4 (increased thermal stability). The decreasing effect of NaClO4 on YADH controlled the thermal stability of the enzyme absolutely and was not compensated by the addition of Na2SO4, a salt which stabilized the enzyme. However, Na2SO4 compensation did occur in response to the decrease in thermal stability caused by (C2H5)4NBr. The rate constants of inactivation by heat (k in) of the enzyme were measured at various temperatures. Effective values of the thermodynamic activation parameters of thermal inactivation, activation of free energy (ΔG ‡), activation enthalpy (ΔH ‡), and activation entropy (ΔS ‡), were determined. The thermal stability of YADH in 0.8 M Na2SO4 increased more than that of pyruvate kinase from Bacillus stearothermophilus, a moderate thermophile. The changes in the values of ΔH ‡ and ΔS ‡ were great and showed a general compensatory tendency, with the exception of in the case of NaClO4. The temperature for the general compensation effect (T c) was approximately 123°C. With Na2SO4, the thermal stability of YADH at a temperature below T c was greater than that in the absence of salt due to the higher values of ΔH ‡ and ΔS ‡, respectively, and thus was an example of low-temperature enzymatic stabilization. With (C2H5)4NBr, the thermal stability of YADH at a temperature below T c was lower than that in the absence of salt due to the lower values of ΔH ‡ and ΔS ‡, respectively, and thus was an example of low-temperature enzymatic destabilization. But with NaClO4, the changes in the values of ΔH ‡ and ΔS ‡ were small and the thermal stability of YADH was thus an example of high-temperature enzymatic destabilization. [ABSTRACT FROM PUBLISHER] |
|
Copyright of Journal of Biochemistry is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
Full Text Finder