Stability of the hydroxynitrile lyase from Hevea brasiliensis: a fluorescence and dynamic light scattering study
| Autor: | Andrea Hickel, Herfried Griengl, Dieter Lehner, Marion Graupner, Albin Hermetter, Otto Glatter |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Hydroxynitrile lyase
biology Chemistry Stereochemistry Fluorescence spectrometry Bioengineering Photochemistry biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Fluorescence Light scattering Fluorescence spectroscopy Enzyme assay Dynamic light scattering biology.protein Hevea brasiliensis Biotechnology |
| Zdroj: | Enzyme and Microbial Technology. 21:361-366 |
| ISSN: | 0141-0229 |
| Popis: | The reasons for the deactivation of the hydroxynitrile lyase (Hnl) from the rubber tree ( Hevea brasiliensis ) at low pH values (below 4.0), and the influence of buffer salts as well as the possible stabilization of the enzyme by additives were investigated. For the elucidation of responsible phenomena, dynamic light scattering and fluorescence spectroscopy were employed. It was found that the Hnl tryptophan fluorescence maximum shifted to a higher wavelength and the anisotropy increased when the pH value was decreased. Furthermore, the aggregate size of the Hnl particles increased with increasing pH; therefore, we suggest an unfolding of the enzyme followed by aggregation leading to closely packed enzyme particles at low pH values. The large particle sizes at high pH are accounted for by the weak interaction of the enzyme molecules which were found not to influence the enzyme activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect