The conditions for immobilizing the new L-aminoacylase-producing bacterial strain, Pseudomonas sp. BA2, by entrapment in i-carrageenan gel, were investigated. The optimal gel concentration and cell load were determined. The addition of and N-acetyl-L-alanine to the immobilizing matrix enhanced CoCl
Production of L-aminoacylase by fermentation of Pseudomonas sp. BA2
✍ Scribed by Antonio Bódalo Santoyo; Josefa Bastida Rodríguez; José Luis Gómez Carrasco; Elisa Gómez Gómez; María Luisa Asanza Teruel; Isabel Alcaraz Rojo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1995
- Tongue
- English
- Weight
- 523 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0268-2575
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✦ Synopsis
The growth and enzymatic production of Pseudomonas sp. BA2, a new L-aminoacylase-producing microorganism, were studied in a bench-top fermenter. Multiple fermentations were carried out in order to determine the optimal pH and temperature values. The influence of the substrate concentration on both growth and L-aminoacylase activity was also investigated. The maximum growth rate and the greatest yield of enzyme were obtained when the fermentation was carried out at pH 7.5, 25°C and DOT > 50%. N-Acetyl-DLalanine, at a concentration of 20 g dm-3, was used as the sole carbon and nitrogen source. The fermentation process provided a maximum biomass concentration of 3.36 g dry weight dm-3. The highest L-aminoacylase production (11429 U g-' dry weight) was obtained after 39 h of cultivation. The results were a significant improvement over those previously reported.
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