Enhanced Performance of Rhizopus oryzae Lipase by Reasonable Immobilization on Magnetic Nanoparticles and Its Application in Synthesis 1,3-Diacyglycerol

Appl Biochem Biotechnol. 2019 Jul;188(3):677-689. doi: 10.1007/s12010-018-02947-2. Epub 2019 Jan 8.

Abstract

Nano-sized Fe3O4 was synthesized by chemical co-precipitation and subsequently modified with 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde to introduce aldehyde group on its surface. With the help of "interface activation" by adding sucrose esters-11 as surfactant, lipase from Rhizopus oryzae was successfully immobilized onto the carrier with great enhancement of activity. The hydrolysis activity of immobilized enzyme were 9.16 times and 31.6 times of free enzyme when p-nitrophenol butyrate and p-nitrophenol palmitate were used as substrates. The thermo-stability of immobilized enzyme was also enhanced compared to free enzyme. The immobilized enzyme was successfully applied in synthesis of 1,3-diacyglycerols (1,3-DAG). The specific esterification activity of immobilized enzyme was about 1.5 times of the free enzyme. The immobilized enzyme showed good region-selectivity towards 1,3-diacyglycerols and retained nearly 80% of its activity after reused for 60 times, revealing a good industrial application prospect.

Keywords: 1,3-diacyglycerols; Immobilization; Interface activated; Nano-sized Fe3O4; Rhizopus oryzae lipase.

MeSH terms

  • Catalysis
  • Diglycerides / chemical synthesis*
  • Enzymes, Immobilized / metabolism*
  • Esterification
  • Kinetics
  • Lipase / metabolism*
  • Magnetite Nanoparticles / chemistry
  • Rhizopus / enzymology*

Substances

  • Diglycerides
  • Enzymes, Immobilized
  • Magnetite Nanoparticles
  • Lipase