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Novel gene estBAS from Bacillus altitudinis, encoding a 216-amino acid esterase (EstBAS) with a signal peptide (SP), was expressed in Escherichia coli. EstBAS∆SP showed the highest activity toward p-nitrophenyl hexanoate at 50 ◦C and pH 8.0 and had a half-life (T1/2) of 6 h at 50 ◦C. EstBAS∆SP was immobilized onto a novel epoxy resin (Lx-105s) with a high loading of 96 mg/g. Fourier transform infrared (FTIR) spectroscopy showed that EstBAS∆SP was successfully immobilized onto Lx-105s. In addition, immobilization improved its enzymatic performance by widening the tolerable ranges of pH and temperature. The optimum temperature of immobilized EstBAS∆SP (Lx-EstBAS∆SP) was higher, 60 ◦C, and overall thermostability improved. T1/2 of Lx-EstBAS∆SP and free EstBAS∆SP at 60 ◦C was 105 and 28 min, respectively. Lx-EstBAS∆SP was used as a biocatalyst to synthesize chloramphenicol palmitate by regioselective modification at the primary hydroxyl group. Conversion efficiency reached 94.7% at 0.15 M substrate concentration after 24 h. Lx-EstBAS∆SP was stable and could be reused for seven cycles, after which it retained over 80% of the original activity.

catalysts

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate