Free and Substrate-Immobilised Lipases from Fusarium verticillioides P24 as a Biocatalyst for Hydrolysis and Transesterification Reactions

Appl Biochem Biotechnol. 2021 Jan;193(1):33-51. doi: 10.1007/s12010-020-03411-w. Epub 2020 Aug 18.

Abstract

Fungal enzymes are widely used in technological processes and have some interesting features to be applied in a variety of biosynthetic courses. Here, free and substrate-immobilised lipases from Fusarium verticillioides P24 were obtained by solid-state fermentation using wheat bran as substrate and fungal carrier. Based on their hydrolytic and transesterification activities, the lipases were characterised as pH-dependent in both reactions, with higher substrate conversion in an alkaline environment. Thermally, the lipases performed well from 30 to 45 °C, being more stable in mild conditions. Organic solvents significantly influenced the lipase selectivity using different vegetable oils as fatty acid source. Omega(ω)-3 production in n-hexane achieved 45% using canola oil, against ≈ 18% in cyclohexane. However, ω-6 production was preferably produced for both solvents using linseed oil with significant alterations in the yield (≈ 79% and 49% for n-hexane and cyclohexane, respectively). Moreover, the greatest enzyme selectivity for ω-6 led us to suppose a lipase preference for the Sn1 position of the triacylglycerol. Lastly, a transesterification reaction was performed, achieving 90% of ester conversion in 72 h. This study reports the characterisation and use of free and substrate-immobilised lipases from Fusarium verticillioides P24 as an economic and efficient method for the first time.

Keywords: Fusarium verticillioides; Hydrolysis; Lipase; Omega-3; Omega-6; Transesterification.

MeSH terms

  • Biocatalysis*
  • Enzymes, Immobilized / chemistry*
  • Esterification
  • Fungal Proteins / chemistry*
  • Fusarium / enzymology*
  • Lipase / chemistry*

Substances

  • Enzymes, Immobilized
  • Fungal Proteins
  • Lipase

Supplementary concepts

  • Fusarium verticillioides