Boosting Enzyme Activity in an Anhydrous Gas Flux with Amphiphilic Polymers

Abstract Gas‐phase enzymatic catalysis offers great potential for both green synthesis and the efficient degradation of volatile chemicals. However, solid enzymes often exhibit extremely low activity compared to their counterparts in native aqueous phase. Although a few immobilization methods have succeeded in increasing activity by preserving enzyme structure, approaches for boosting enzyme activity remain underdeveloped. In this study, we propose a general and facile method to boost enzyme activity in the gas phase, which utilizes amphiphilic polymers to energize enzyme conformational dynamics and thus enhance enzyme catalysis kinetics. The triblock copolymer Pluronics with low melting points were co‐lyophilized with Candida antarctica lipase B (CalB), yielding Pluronic/CalB powders that appeared a 70‐fold increase in activity compared to free CalB powder. Low‐field nuclear magnetic resonance (LF‐NMR), solid‐state nuclear magnetic resonance (ssNMR) and dielectric relaxation spectroscopy identified the enhancement of enzyme dynamics on the µs–ms timescale, whereas Fourier transform infrared spectroscopy (FTIR) detected structural perturbations of the native enzyme in Pluronic/CalB. The apparent activity of the enzyme/polymer powders correlated positively with both enzyme dynamics and polymer flexibility. These findings provide new molecular physical insights into gas‐phase enzyme catalysis, which are essential for advancing enzyme applications in nonnatural scenario.