info:eu-repo/semantics/article
Engineering the Performance of Artificial Inclusion Bodies Built of Catalytic β-Galactosidase
Fecha
2021-02-01Registro en:
Sanchez, Julieta Maria; López Laguna, Hèctor; Serna, Naroa; Unzueta, Ugutz; Clop, Pedro Diego; et al.; Engineering the Performance of Artificial Inclusion Bodies Built of Catalytic β-Galactosidase; American Chemical Society Inc; ACS Sustainable Chemistry and Engineering; 9; 6; 1-2-2021; 2552-2558
2168-0485
CONICET Digital
CONICET
Autor
Sanchez, Julieta Maria
López Laguna, Hèctor
Serna, Naroa
Unzueta, Ugutz
Clop, Pedro Diego
Villaverde Corrales, Antonio
Vazquez, Esther
Resumen
One of the most critical bottlenecks in the application of industrial enzymes is the preservation of protein stability throughout the catalytic reaction, which often requires protein engineering and/or process optimization. In this context, we have designed and deeply characterized an efficient, stable, and reusable enzymatic platform based on the Escherichia coli β-galactosidase. The enzyme was assembled in vitro, by using divalent cations as molecular linkers, as stable protein microparticles showing catalytic activity. In this assembled microstructure, β-galactosidase exhibits a particular conformation within the microparticles, sharing structural traits (a high cross-parallel beta-sheet content) with the bacterial inclusion bodies and secretory amyloids from the mammalian endocrine system. This fact confers enhanced thermal stability compared to the soluble protein version and ensures high reusability in industry-oriented processes. On the other hand, among the catalog of cations tested as molecular linkers, a mixture of Ca2+ and Mg2+ offers the best performance to the catalytic particle. Altogether, these data offer clues for the application of a self-immobilized enzymatic platform with transversal applicability and enormous potential in biotechnology and biomedicine.