Premium
Production of optically pure L ‐alanine by immobilized Pseudomonas sp. BA2 cells
Author(s) -
Bódalo Santoyo Antonio,
Bastida Rodríguez Josefa,
Gómez Carrasco José Luis,
Gómez Gómez Elisa,
Alcaraz Rojo Isabel,
Asanza Teruel María Luisa
Publication year - 1998
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(1998110)73:3<197::aid-jctb946>3.0.co;2-s
Subject(s) - chemistry , pseudomonas , substrate (aquarium) , tris , alanine , enzyme , chromatography , nuclear chemistry , strain (injury) , bacteria , biochemistry , amino acid , biology , ecology , genetics , anatomy
The conditions for immobilizing the new L ‐aminoacylase‐producing bacterial strain, Pseudomonas sp. BA2, by entrapment in κ‐carrageenan gel, were investigated. The optimal gel concentration and cell load were determined. The addition of CoCl 2 and N ‐acetyl‐ L ‐alanine to the immobilizing matrix enhanced L ‐aminoacylase activity. The enzymatic properties of immobilized Pseudomonas sp. BA2 were investigated. Enzyme activity in immobilized cells was optimal at a pH of 6·5 using 0·15 mol dm −3 Tris–maleate buffer at 45°C. The presence of 0·7 mmol dm −3 CoCl 2 in the enzymatic reaction mixture improved L ‐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 0·74 mol h −1 g cell −1 dm −3 which is noticeably higher than that previously reported in the literature. © 1998 Society of Chemical Industry