Lipase-catalyzed production of pyridoxine monolaurate in solvent-free bioreactor system

Food Chem. 2023 Jan 15:399:133949. doi: 10.1016/j.foodchem.2022.133949. Epub 2022 Aug 17.

Abstract

This study demonstrated that solvent-free gas bubbling system enhanced production efficiency of pyridoxine monolaurate in the esterification catalyzed by immobilized Candida antarctica lipase B (Lipozyme 435). Volumetric productivity in solvent-free gas bubbling system (41.24 mmol/L/h) was 3.7 and 2.1-fold higher than those in conventional organic solvent system (11.10 mmol/L/h) and solvent-free system (19.86 mmol/L/h) using magnetic stirring, respectively. Among the three bioreactor systems, solvent-free gas bubbling system provided the best reusability of the lipase retaining 94.45 % of initial activity for six batch reactions. In the bioreactor system, 5-O-lauroyl-pyridoxine was regioselectively produced with maximum production of 371.17 mmol/L at 70 °C and 0.10 of substrate molar ratio ([pyridoxine]/[lauric acid]) for 9 h. Pyridoxine monolaurate exhibited interfacial activity at oil-water interfaces, suggesting it had emulsifying properties. Pyridoxine monolaurate is expected to be applied as a multi-functional emulsifier with nutritional values to replace both small molecule emulsifiers and pyridoxine hydrochloride in fortified beverages.

Keywords: Immobilized lipase; Interfacial activity; Multi-functional emulsifier; Pyridoxine fatty acid esters; Regioselectivity; Solvent-free esterification.

MeSH terms

  • Bioreactors
  • Catalysis
  • Enzymes, Immobilized* / chemistry
  • Esterification
  • Lipase / metabolism
  • Pyridoxine*
  • Solvents / chemistry

Substances

  • Enzymes, Immobilized
  • Solvents
  • Lipase
  • Pyridoxine