Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials

The use of light as an external stimulus to control the enzyme activity is an emerging strategy that enables accurate, remote, and noninvasive biotransformations. In this context, immobilization of enzymes on plasmonic nanoparticles offers an opportunity to create light-responsive biocatalytic materials. Nevertheless, a fundamental and mechanistic understanding of the effects of localized surface plasmon resonance (LSPR) excitation on enzyme regulation remains elusive. We herein investigate the plasmonic effects on biocatalysis using Au nanospheres (AuNSp) and nanostars (AuNSt) as model plasmonic nanoparticles, lipase from Candida antarctica fraction B (CALB) as a proof-of-concept enzyme, and 808 nm as near-infrared light excitation. Our data show that LSPR excitation enables an enhancement of 58% in the enzyme activity for CALB adsorbed on AuNSt, compared with the dark conditions. This work shows how photothermal heating over the LSPR excitation enhances the CALB activity through favoring product release in the last step of the enzyme mechanism. We propose that the results reported herein shed important mechanistic and kinetic insights into the field of plasmonic biocatalysis and may inspire the rational development of plasmonic nanomaterial-enzyme hybrids with tailored activities under external light irradiation.