Efficient production of peracetic acid in aqueous solution with cephalosporin-deacetylating acetyl xylan esterase from Bacillus subtilis
•Acetyl xylan esterase (AXE) from Bacillus subtilis CICC 20034 exhibited significant perhydrolase activity.•AXE could be efficiently produced in a low-cost medium.•The highest concentration of enzyme-catalyzed peracetic acid (PAA) produced was about 150 mM.•Immobilized AXE could be efficiently reused for 10 cycles.
Peracetic acid (PAA) is widely used in sterilization, bleaching textile industry, environmental engineering, chemical synthesis, and biomimetic chemistry. A previous study reported that acetyl xylan esterase (AXE) of Bacillus subtilis CICC 20034 has high activity toward cephalosporin C and 7-aminocephalosporanic acid. In this study, we found that AXE also exhibited high perhydrolysis activity toward acetate esters and endowed itself with great industrial interest on enzyme-catalyzed preparation of PAA. Recombinant AXE of B. subtilis CICC 20034 could be efficiently produced in a low-cost autoinduction medium with an activity of 6.8 × 103 U/mL. The reaction conditions for the optimal synthesis of PAA were as follows: 0.30 mg/mL AXE crude enzyme, 300 mM glycerol triacetate, and 1 M hydrogen peroxide, pH 8.0, and 20 °C, which produced approximately 150 mM of PAA within 5 min. The AXE was then immobilized on an acrylate amino resin; the activity of the immobilized AXE was 383.7 U/g. In the presence of 1 g/mL of immobilized AXE resin, PAA titer of the initial reaction batch was approximately 142.5 mM, and about 95.5 mM of PAA could be produced after 10 cycles.
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Journal: Process Biochemistry - Volume 50, Issue 12, December 2015, Pages 2121–2127