Enzymatic interfacial conversion of acylglycerols in Pickering emulsions stabilized by hydrogel microparticles

J Colloid Interface Sci. 2024 May:661:228-236. doi: 10.1016/j.jcis.2024.01.192. Epub 2024 Jan 28.

Abstract

Hypothesis: A critical challenge in the enzymatic conversion of acylglycerols is the limited exposure of the enzyme dissolved in the aqueous solution to the hydrophobic substrate in the oil phase. Positioning the enzyme in a microenvironment with balanced hydrophobicity and hydrophilicity in Pickering emulsion will facilitate the acylglycerol-catalyzing reactions at the interface between the oil and liquid phases.

Experiments: In this work, to overcome the challenge of biphasic catalysis, we report a method to immobilize enzymes in polyethylene glycol (PEG)-based hydrogel microparticles (HMPs) at the interface between the oil and water phases in Pickering emulsion to promote the enzymatic conversion of acylglycerols.

Findings: 3 wt% of HMPs can stabilize the oil-in-water Pickering emulsion for at least 14 days and increase the viscosity of emulsions. Lipase-HMP conjugates showed significantly higher hydrolytic activity in Pickering emulsion; HMP-immobilized lipase SMG1 showed an activity about three times that of free lipase SMG1. Co-immobilization of a lipase and a fatty acid photodecarboxylase from Chlorella variabilis (CvFAP) in Pickering emulsion enables light-driven cascade conversion of triacylglycerols to hydrocarbons, transforming waste oil to renewable biofuels in a green and sustainable approach. HMPs stabilize the Pickering emulsion and promote interfacial biocatalysis in converting acylglycerols to renewable biofuels.

Keywords: Enzyme immobilization; Fatty acid photodecarboxylase; Hydrogel microparticles; Lipase; Pickering emulsion interfacial biocatalysis.

MeSH terms

  • Biofuels
  • Chlorella*
  • Emulsions / chemistry
  • Glycerides*
  • Hydrogels
  • Lipase / chemistry

Substances

  • Glycerides
  • Emulsions
  • Hydrogels
  • Biofuels
  • Lipase