We successfully produced purified and identified active laccases of E. coli BL21(CueO named ECOL), Bacillus pumilus DSM 27 laccase (CotA named BPUL), Bacillus halodurans C-125 laccase (Lbh1 named BHAL) and Thermus thermophilus HB27 (tthL named TTHL).
We successfully designed a shuttle vector for site-directed integration in P. pastoris which allows the production and secretion of a protein of interest.
We established a method for the degradation of several compounds with the help of our self-produced laccases. The LC-MS and HPLC analysis showed that our laccases are able to degrade the hormonal substrates estradiol, estrone and ethinyl estradiol.
We successfully immobilized Trametes versicolor-laccase (named TVEL0), E. coli BL21-laccase (CueO named ECOL) and Bacillus pumilus DSM 27-laccase (CotA named BPUL) and measured their activity.
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