The thermodynamic stability of lipases and proteases from psychrotrophic bacteria
| Autor: | Richard K. Owusu, JS Knapp, A. Makhzoum |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
chemistry.chemical_classification
Proteases Chromatography biology Chemistry Stereochemistry Thermophile Pseudomonas fluorescens General Medicine biology.organism_classification medicine.disease_cause Analytical Chemistry Enzyme Psychrotrophic bacteria medicine Denaturation (biochemistry) Chemical stability Thermolabile Food Science |
| Zdroj: | Food Chemistry. 39:187-195 |
| ISSN: | 0308-8146 |
| Popis: | The thermodynamic or conformational stability of psychrotroph lipases and proteases, measured as the Gibbs free energy difference (ΔG ⊖ ) between the native and denatured enzymes, were estimated from enzyme temperature-activity profile data. ΔG ⊖ estimates of 8–10 kJ/mol and 16–17 kJ/mol were obtained for psychrotroph-derived lipases and proteases, respectively. Pseudomonas fluorescens strain AR-11 protease was unusually thermolabile ( Δ G ⊖ = 3·0–7·6 kJ / mol ). These values were compared with values for some mesophilic and thermophilic enzymes and the possible relationship of ΔG ⊖ to psychrotrophic enzyme heat-resistance is discussed. |
| Databáze: | OpenAIRE |
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