Operational Stability of Enzymes
| Autor: | Karlheinz Dr Drauz, Christian Wandrey, Herbert Klenk, Andreas S. Bommarius |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
inorganic chemicals
Protein Denaturation Stereochemistry Cations Divalent Swine Aspergillus oryzae Continuous stirred-tank reactor Stereoisomerism Kidney General Biochemistry Genetics and Molecular Biology Catalysis Amidohydrolases Enzyme activator History and Philosophy of Science Organic chemistry Animals Amino Acids Operational stability chemistry.chemical_classification biology Continuous reactor General Neuroscience biology.organism_classification Amino acid Enzyme Activation Enzyme chemistry Biochemical engineering |
| Zdroj: | Annals of the New York Academy of Sciences. 672:126-136 |
| ISSN: | 1749-6632 0077-8923 |
| DOI: | 10.1111/j.1749-6632.1992.tb35613.x |
| Popis: | The method of measuring enzyme deactivation by monitoring necessary addition of fresh enzyme to keep a constant degree of conversion in a CSTR at constant [E] x tau, the product of concentration of active enzyme [E] and residence time tau, was successfully applied to acylase I from porcine kidney and Aspergillus oryzae fungus. Fungal enzyme was found to be more stable than kidney enzyme. Activation by both Co2+ and Zn2+ ions also yielded increased operational enzyme stability: Co2+ and Zn2+ are better stabilizers than activators. Mg2+ and Ca2+ are found to be neither activators nor stabilizers. Fungal acylase partially deactivated by exposition to a metal-free medium in the CSTR was reactivated by addition of Zn2+, demonstrating that loss of Zn2+ from the enzyme molecule is mainly responsible for deactivation in a continuous reactor. |
| Databáze: | OpenAIRE |
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