Cryogenic activity and stability of benzaldehyde lyase enzyme in lipidic mesophases-nanoconfined water.

Tao Zhou,Yang Yao,Raffaele Mezzenga,Qin Zhang

doi:10.1039/d1cc01315g

Abstract

Phytantriol-based lipidic mesophases (LMs) are introduced as a platform for cryoenzymology, which relies on the presence of liquid water in LMs at subzero temperatures. After incorporation into LMs, the model enzyme Benzaldehyde lyase (BAL) shows high cryogenic stability and activity. In contrast, BAL in bulk solution undergoes significant secondary structural transitions caused by low temperatures (cold denaturation), demonstrating the potential of this approach to enable in meso cryoenzymology.

Highlights

Phytantriol-based lipidic mesophases (LMs) are introduced as a platform for cryoenzymology, which relies on the presence of liquid water in LMs at subzero temperatures
Benzaldehyde lyase (BAL) in bulk solution undergoes significant secondary structural transitions caused by low temperatures, demonstrating the potential of this approach to enable in meso cryoenzymology
The application of LMs as a cryoenzymology host has become feasible by the recent finding, in our group, of a novel unfrozen lipid which allows the water confined in LMs produced using this lipid, to resist crystallization at temperatures as low as 10 K.26

Summary

Introduction

Phytantriol-based lipidic mesophases (LMs) are introduced as a platform for cryoenzymology, which relies on the presence of liquid water in LMs at subzero temperatures. The access to cryoenzymatic reactions in phytantriol-based LMs relies on the existence of water at subzero temperatures, as demonstrated by differential scanning calorimetry (DSC) measurements and already reported in our recent work.[27] Water confined in Phy70–W30 (mixture of 70 wt% phytantriol and 30 wt% water) with BAL enzyme and NA substrates incorporated within, could remain completely unfrozen down to À15 1C.

Results

Conclusion