期刊
ACS SUSTAINABLE CHEMISTRY & ENGINEERING
卷 9, 期 6, 页码 2552-2558出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssuschemeng.0c08345
关键词
artificial inclusion bodies; catalytic microparticles; reusability; thermostability
资金
- Fondo Europeo de Desarrollo Regional (FEDER) [PID2019 105416RB-I00/AEI/10.13039/501100011033]
- AGAUR [2019FI_B00352, 2017SGR-229]
- VI National R&D&I Plan 2008-2011
- Iniciativa Ingenio 2010, Consolider Program, CIBER Actions
- Instituto de Salud Carlos III
- European Regional Development Fund
- ICREA ACADEMIA award
- Miguel Servet contract from ISCIII - European Social Fund (ESF investing in your future) [CP19/00028]
A self-immobilized enzymatic platform based on Escherichia coli beta-galactosidase was designed, showing enhanced thermal stability and high reusability. The use of divalent cations as molecular linkers in assembling stable protein microparticles offered efficient catalytic performance. The platform presents transversal applicability and great potential in biotechnology and biomedicine.
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 beta-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, beta-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.
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