Secondary Structure and Stability of Marsh Grapefruit Thermolabile Pectinesterase
| Autor: | D. Sun, T. Grant, Louise Wicker, L. Dure |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Chromatography Environmental factor General Chemistry medicine.disease_cause Pectinesterase Enzyme chemistry medicine Protein precipitation Denaturation (biochemistry) Thermolabile General Agricultural and Biological Sciences Protein secondary structure Nuclear chemistry |
| Zdroj: | Journal of Agricultural and Food Chemistry. 46:3480-3483 |
| ISSN: | 1520-5118 0021-8561 |
| Popis: | Thermolabile pectinesterase (TL-PE) was inactivated completely after 8 h of dialysis at pH 3.3 but retained activity at pH 4.1 and pH 7.0. Circular dichroism (CD) spectra and secondary structural analysis showed similar secondary structure between pH 7.0, pH 4.1, and pH 3.3. The CD spectra of TL-PE were compared at pH 7.0 and 4.1 and between 25 and 70 °C. Heating TL-PE at pH 7.0 and 4.1 resulted in irreversible protein precipitation. The thermal transition temperature for destabilization of TL-PE structure occurs at a lower temperature at pH 4.1 than at pH 7.0, suggesting some change in the secondary structure of TL-PE. Keywords: Pectinesterase; stability; activity; thermal transition; denaturation |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|