Characteration of a novel arylesterase from probiotics GG with the preference for medium- and long-chain -Nitrophenyl esters.

Unlabelled: We prospected a novel arylesterase LggEst from the probiotics s GG by genome mining strategy, and characterized the enzymatic properties in detail. Biochemical characterization revealed that arylesterase LggEst presented high activity at a wide range of temperatures from 25 to 65 °C with maximum activity at 50 °C. LggEst maintained high activity in the pH range from 5.5 to 7.5 with optimum pH of 6.5. LggEst might efficiently hydrolyze a series of aryl substrates -nitrophenyl esters with different acyl chain lengths. LggEst displayed the V from 2.8 to 77.3 μmol min mg protein and the from 1.8 to 48.8 s with the highest catalytic activity on NPC6. The of LggEst on different substrates varied significantly from 4.9 μM to 5.6 mM with the highest affinity on NPC10. LggEst exhibited the preference for medium- and long-chain -nitrophenyl ester. LggEst showed remarkable thermostability at 45 °C. LggEst could be tolerant of several organic solvents at the concentration of 10% and DMSO and methanol at the concentration of 20%. Catalytic activity of LggEst was improved by 12% in the presence of 20% ethylene glycol. LggEst was resistant to high concentrations of sodium citrate and sodium chloride. Notably, enzymatic activity of LggEst was significantly enhanced in the presence of 0.1% sodium deoxycholate at high temperatures.

Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-021-03053-7.