Immobilised Enzymes for Sesquiterpene Synthesis in Batch and Flow Systems

Graphical Abstract

Sesquiterpene synthase immobilisation on controlled porosity glass through metal-ion affinity binding is exploited. This strategy improves enzyme reusability and allows for easier downstream processing and the development of continuous flow processes.

Abstract

Sesquiterpene synthases catalyse the bioconversion of farnesyl diphosphate into sesquiterpenes. The immobilisation of sesquiterpene synthases on controlled porosity glass through metal-ion affinity binding is reported. The immobilised sesquiterpene synthases were able to maintain 50 % catalytic activity for at least 50 cycles under continuous flow conditions.