Production of optically pure L-alanine by immobilized Pseudomonas sp. BA2 cells

✍ Scribed by Antonio Bódalo Santoyo; Josefa Bastida Rodríguez; José Luis Gómez Carrasco; Elisa Gómez Gómez; Isabel Alcaraz Rojo; María Luisa Asanza Teruel

• Publisher: Wiley (John Wiley & Sons)
• Year: 1998
• Tongue: English
• Weight: 228 KB
• Volume: 73
• Category: Article
• ISSN: 0268-2575
• DOI: 10.1002/(sici)1097-4660(1998110)73:3<197::aid-jctb946>3.0.co;2-s

✦ Synopsis

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 2 L-aminoacylase activity. The enzymatic properties of immobilized Pseudomonas sp. BA2 were investigated. Enzyme activity in immobilized cells was optimal at a pH of 6É5 using 0É15 mol dm~3 TrisÈmaleate bu †er at 45¡C. The presence of 0É7 mmol dm~3 in the enzymatic reaction mixture improved L-CoCl 2 aminoacylase activity. The immobilized cell preparation was used for the production of L-alanine from N-acetyl-DL-alanine in a batch reactor. Conversions of 100% were obtained using substrate concentrations ranging from 20 to 200 mmol dm~3. The reactor production was 0É74 mol h~1 g cell~1 dm~3 which is noticeably higher than that previously reported in the literature. 1998