Optimization of an industrial biocatalyst of glutaryl acylase: stabilization of the enzyme by multipoint covalent attachment onto new amino-epoxy Sepabeads.

@article{LpezGallego2004OptimizationOA,
  title={Optimization of an industrial biocatalyst of glutaryl acylase: stabilization of the enzyme by multipoint covalent attachment onto new amino-epoxy Sepabeads.},
  author={Fernando L{\'o}pez-Gallego and Lorena Betancor and Aurelio Hidalgo and C{\'e}sar Mateo and Jos{\'e} M Guis{\'a}n and Roberto Fernandez-Lafuente},
  journal={Journal of biotechnology},
  year={2004},
  volume={111 2},
  pages={
          219-27
        }
}
Glutaryl-7-aminocephalosporanic acid acylase (GA), an industrially relevant enzyme, has been immobilized onto very different supports, including glyoxyl agarose, heterofunctional epoxy Sepabeads, glutaraldehyde and cyanogen bromide (CNBr) activated supports. Immobilization onto amino-epoxy Sepabeads rendered the most thermo stable preparation of GA, with a half-life time eight times higher than the soluble enzyme, keeping 80% of the enzyme activity. Several parameters that affect the enzyme… CONTINUE READING