Production of hydroxamic acids by immobilized Pseudomonas aeruginosa cells Kinetic analysis in reverse micelles
| Autor: | Rita Pacheco, Amin Karmali, Marisa Bernardo, Maria Luísa Serralheiro |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Media
Acyltransferase Bioengineering Biochemistry Micelle Catalysis Amidase Reaction rate Hydrolysis chemistry.chemical_compound Organic chemistry Purification chemistry.chemical_classification Inhibitors Process Chemistry and Technology equipment and supplies Hydroxamic acids Amino acid chemistry Biocatalysis Acrylamide Pseudomonas aeruginosa Acetamide Reverse micelles |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| Popis: | Intact cells from Pseudomonas aeruginosa strain L10 containing amidase were used as biocatalysts both free and immobilized in a reverse micellar system. The apparent kinetic constants for the transamidation reaction in hydroxamic acids synthesis, were determined using substrates such as aliphatic, amino acid and aromatic amides and esters, in both media. In reverse micelles, K m values decreased 2–7 fold relatively to the free biocatalyst using as substrates acetamide, acrylamide, propionamide and glycinamide ethyl ester. We have concluded that overall the affinity of the biocatalyst to each substrate increases when reactions are performed in the reversed micellar system as opposed to the buffer system. The immobilized biocatalyst in general, exhibits higher stability and faster rates of reactions at lower substrates concentration relatively to the free form, which is advantageous. Additionally, the immobilization revealed to be suitable for obtaining the highest yields of hydroxamic acids derivatives, in some cases higher than 80%. |
| Databáze: | OpenAIRE |
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