Enhanced triolein and ethyl ferulate interesterification performance by CRL-AuNPs

Bioresour Technol. 2024 May:399:130599. doi: 10.1016/j.biortech.2024.130599. Epub 2024 Mar 15.

Abstract

This study established a Candida rugosa lipase (CRL) system to catalyze triolein and ethyl ferulate interesterification. The products were identified, and the binding mode between the substrates and CRL was predicted through molecular docking. Three methods for preparing CRL-AuNPs were proposed and characterized. It was found that the addition of 40 mL of 15 nm gold nanoparticles increased the CRL activity from 3.05 U/mg to 4.75 U/mg, but the hybridization efficiency was only 32.7 %. By using 4 mL of 0.1 mg/mL chloroauric acid, the hybridization efficiency was improved to 50.7 %, but the enzyme activity was sharply decreased. However, when the molar ratio of Mb to HAuCl4 was 0.2, the hybridization efficiency increased to 71.8 %, and the CRL activity was also enhanced to 5.98 U/mg. Under optimal conditions, the enzyme activity of CRL-AuNPs③ was maintained at 95 % after 6 repetitions and 85.6 % after 30 days at room temperature.

Keywords: CRL-AuNPs; Hybridization; Lipase; Methanobactin; Nanogold.

MeSH terms

  • Caffeic Acids*
  • Candida / metabolism
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism
  • Gold
  • Lipase* / metabolism
  • Metal Nanoparticles*
  • Molecular Docking Simulation
  • Saccharomycetales*
  • Triolein

Substances

  • Lipase
  • Gold
  • Enzymes, Immobilized
  • Triolein
  • ethyl ferulate
  • Caffeic Acids

Supplementary concepts

  • Diutina rugosa