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

Abstract

The use of light as an external stimulus to control 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 on the effects of localized surface plasmon resonance (LSPR) excitation over enzyme regulation remains elusive. We investigate herein 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 NIR light excitation. Our data show that LSPR excitation enables an enhancement of 58% in enzyme activity for CALB adsorbed on AuNSt, compared with the dark conditions. This work shows how photothermal heating over the LSPR excitation enhances 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 in the field of plasmonic biocatalysis and may inspire the rational development of plasmonic nanomaterial-enzyme hybrids with tailored activities under external light irradiation.

Stimuli-Responsive Regulation of Biocatalysis through Metallic Nanoparticle Interaction

“…30 The photothermal enhancement of biocatalytic activity using a conventional enzyme (lipase from Candida antarctica fraction B (CALB)) without the need for a matrix was very recently reported through their adsorption on Au nanostars and upon light irradiation (Figure 1C). 31 In this way, the evolution of these studies reveals rapid progress in the field and promising studies to come in the foreseeable future.…”

Trends in Sustainable Synthesis of Organics by Gold Nanoparticles Embedded in Polymer Matrices

“…The presence of polymer chains under gel-like conditions allows for the nucleation stage and slows down the growth of the particles or their coalescence. Synthetic and natural polymers have been extensively used as stabilizer of AuNPs: poly(N-vinyl-2-pyrrolidone) [27], polyacrylates [28,29], poly(ethylene glycol), alginate [30,31], polysaccharides [32], chitosan [33,34], polystyrenes [35,36], polystyrene-polybutadiene block copolymers [37], poloxamers block copolymers [38][39][40], poly(ε-caprolactone)-poly(Nvinyl-2-pyrrolidone) block copolymers [41], poly(ethylene glycol)-polyethylenimine-poly(εcaprolactone) [42], poly(ethylene glycol)-poly(vinyl alcohol) block copolymers [43], redoxactive polymers [44], negatively charged polyelectrolytes such copolymers of 4-styrenesulfonate and maleic acid (P(SS-co-MA) [45], and biomacromolecules such as bovine serum albumin [46] or enzymes [47].…”

Protein-based (bio)materials: a way toward high-performance graphene enzymatic biosensors

“…Scaffold materials are usually natural polymers ( e.g. , cellulose, chitosan, agarose, and proteins), 7–13 synthetic polymers, 14–16 metallic 17,18 and polymeric nanoparticles, 19,20 hydrogels, 21,22 silica, 23–25 and metal–organic frameworks. 26–29…”

“…Scaffold materials are usually natural polymers (e.g., cellulose, chitosan, agarose, and proteins), [7][8][9][10][11][12][13] synthetic polymers, [14][15][16] metallic 17,18 and polymeric nanoparticles, 19,20 hydrogels, 21,22 silica, [23][24][25] and metal-organic frameworks. [26][27][28][29] The sensitivity and overall performance of enzymatic biosensors can be improved tremendously as a result of the incorporation of carbon nanomaterials (CNM) in their fabrication.…”