Immobilization of GH78 α-L-Rhamnosidase from Thermotoga petrophilea with High-Temperature-Resistant Magnetic Particles Fe3O4-SiO2-NH2-Cellu-ZIF8 and Its Application in the Production of Prunin Form Naringin

J Microbiol Biotechnol. 2021 Mar 28;31(3):419-428. doi: 10.4014/jmb.2004.04055.

Abstract

To efficiently recycle GH78 thermostable rhamnosidase (TpeRha) and easily separate it from the reaction mixture and furtherly improve the enzyme properties, the magnetic particle Fe3O4-SiO2-NH2-Cellu-ZIF8 (FSNcZ8) was prepared by modifying Fe3O4-NH2 with tetraethyl silicate (TEOS), microcrystalline cellulose and zinc nitrate hexahydrate. FSNcZ8 displayed better magnetic stability and higher-temperature stability than unmodified Fe3O4-NH2 (FN), and it was used to adsorb and immobilize TpeRha from Thermotoga petrophilea 13995. As for properties, FSNcZ8-TpeRha showed optimal reaction temperature and pH of 90°C and 5.0, while its highest activity approached 714 U/g. In addition, FSNcZ8-TpeRha had better higher-temperature stability than FN. After incubation at 80°C for 3 h, the residual enzyme activities of FSNcZ8-TpeRha, FN-TpeRha and free enzyme were 93.5%, 63.32%, and 62.77%, respectively. The organic solvent tolerance and the monosaccharides tolerance of FSNcZ8-TpeRha, compared with free TpeRha, were greatly improved. Using naringin (1 mmol/l) as the substrate, the optimal conversion conditions were as follows: FSNcZ8-TpeRha concentration was 6 U/ml; induction temperature was 80°C; the pH was 5.5; induction time was 30 min, and the yield of products was the same as free enzyme. After repeating the reaction 10 times, the conversion of naringin remained above 80%, showing great improvement of the catalytic efficiency and repeated utilization of the immobilized α-L-rhamnosidase.

Keywords: Immobilization; alpha-L-rhamnosidase; magnetic microspheres; naringin; reusability.

MeSH terms

  • Adsorption
  • Bacterial Proteins / chemistry
  • Biocatalysis
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Flavanones / metabolism*
  • Glycoside Hydrolases / chemistry*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Magnetic Phenomena
  • Magnetite Nanoparticles / chemistry*
  • Phlorhizin / analogs & derivatives*
  • Phlorhizin / biosynthesis
  • Recombinant Proteins / chemistry
  • Thermotoga / enzymology

Substances

  • Bacterial Proteins
  • Enzymes, Immobilized
  • Flavanones
  • Magnetite Nanoparticles
  • Recombinant Proteins
  • prunin
  • Phlorhizin
  • Glycoside Hydrolases
  • alpha-L-rhamnosidase
  • naringin