Lipase Catalyzed Transesterification of Model Long-Chain Molecules in Double-Shell Cellulose-Coated Oil-in-Water...

Area of Science:

• Biocatalysis
• Green Chemistry
• Materials Science

Background:

• Lipase-catalyzed transesterification offers a sustainable alternative to chemical catalysis but is limited by low efficiency in biphasic systems due to restricted interfacial area.
• Emulsion particles can enhance surface area and activity, but integrating enzymes effectively remains a challenge.

Purpose of the Study:

• To investigate cellulose as a natural surfactant for creating oil-in-water emulsions.
• To evaluate the ability of lipase, introduced into the aqueous phase, to integrate with cellulose-coated emulsion microparticles and catalyze transesterification.

Main Methods:

• Utilized cellulose to form oil-in-water emulsions.
• Introduced lipase into the aqueous phase of the emulsions.
• Characterized emulsion particle morphology using light, fluorescence, and cryogenic scanning electron microscopy.
• Assessed lipase activity via hydrolysis of emulsified p-nitrophenyl dodecanoate and transesterification of emulsified methyl laurate and oleyl alcohol.

Main Results:

• Cellulose-coated emulsion particles exhibited a complex structure, confirmed by microscopy.
• Lipase successfully penetrated the emulsion particles and localized at the oil core interface.
• Demonstrated effective lipase catalysis for transesterification within the emulsion microparticles.
• Observed preferential transesterification over hydrolysis despite the presence of water.

Conclusions:

• Cellulose-based emulsion particles provide an effective platform for enhancing lipase-catalyzed transesterification.
• Lipase integration and activity within these microparticles are feasible, overcoming limitations of traditional biphasic systems.
• This approach offers a promising strategy for efficient and green biocatalysis in industrial applications.