INTEC   05402
INSTITUTO DE DESARROLLO TECNOLOGICO PARA LA INDUSTRIA QUIMICA
Unidad Ejecutora - UE
artículos
Título:
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l -arabinose isomerase through multipoint covalent attachment approach
Autor/es:
MANZO, RICARDO M.; DE SOUSA, MARYLANE; FENOGLIO, CECILIA L.; ROCHA BARRO GONÇALVES, LUCIANA; MAMMARELLA, ENRIQUE J.
Revista:
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
Editorial:
SPRINGER HEIDELBERG
Referencias:
Lugar: HEIDELBERG; Año: 2015 vol. 42 p. 1325 - 1340
ISSN:
1367-5435
Resumen:
D-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others.This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achievedby reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U g−1 gel with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave anapparent activity of 161.8 U g−1 gel with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategyto obtain high active L-AI insolubilized derivatives.