التفاصيل البيبلوغرافية
| العنوان: |
Stabilization of galactose oxidase by high hydrostatic pressure: Insights on the role of cavities size |
| المؤلفون: |
Kang, Min J., Reyes‐De‐Corcuera, José I. |
| المساهمون: |
U.S. Department of Agriculture, National Institute of Food and Agriculture |
| المصدر: |
Biotechnology and Bioengineering ; ISSN 0006-3592 1097-0290 |
| بيانات النشر: |
Wiley |
| سنة النشر: |
2024 |
| المجموعة: |
Wiley Online Library (Open Access Articles via Crossref) |
| الوصف: |
High hydrostatic pressure stabilized galactose oxidase (GaOx) at 70.0–80.0°C against thermal inactivation. The pseudo‐first‐order rate constant of inactivation k inact decreased by a factor of 8 at 80°C and by a factor of 44 at 72.5°C. The most pronounced effect of pressure was at the lowest studied temperature of 70.0°C with an activation volume of inactivation Δ V ‡ of 78.8 cm 3 mol −1 . The optimal pressure against thermal inactivation was between 200 and 300 MPa. Unlike other enzymes, as temperature increased the ΔV ‡ of inactivation decreased, and as pressure increased the activation energy of inactivation E ai increased. Combining the results for GaOx with earlier research on the pressure‐induced stabilization of other enzymes suggests that Δ V ‡ of inactivation correlates with the total molar volume of cavities larger than ~100 Å 3 in enzyme monomers for enzymes near the optimal pH and whose thermal unfolding is not accompanied by oligomer dissociation. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| DOI: |
10.1002/bit.28715 |
| الإتاحة: |
https://doi.org/10.1002/bit.28715Test |
| حقوق: |
http://onlinelibrary.wiley.com/termsAndConditions#amTest ; http://onlinelibrary.wiley.com/termsAndConditions#vorTest |
| رقم الانضمام: |
edsbas.A4432465 |
| قاعدة البيانات: |
BASE |
