Expression and characterization of an alkaline esterase from marine Acinetobacter sp.

Abstract:

[Objective] The gene encoding estA in a strain of Acinetobacter sp. screened from abalone visceral was cloned and expressed in Pichia pastoris. [Methods] The estA gene was amplified and integrated into the genome of P. pastoris X33 via the pPICZα-C vector. The recombinant estA was expressed into the culture medium, and the recombinant protein were purified and characterized. [Results] The estA gene of 912 bp was cloned. After induced with methanol, recombinant esterase reached 1 200 U/L with weight of 33.7 kD. The optimum pH and temperature of recombinant esterase were 8.0 and 40 °C, respectively. Furthermore, this esterase exhibited remarkable stability at pH between 8.0?10.0 and under 60 °C. [Conclusion] The gene of estA from Acinetobacter sp. was successfully cloned and expressed in P. pastoris.