Synthesis of(4S)-tetrahydronaphthalone catalyzed by immobilized Pseudovibrio-ω-aminotransferase
The self-assembly immobilization of Pseudovibrio-ω-transaminase(P-ω-TA)was explored using bacteriophage T4 capsid as carrier.Fusion of P-ω-TA to the non-essential small outer capsid protein(Soc)of bacteriophage T4 led to the affinity immobilization of P-ω-TA on the T4 capsid with a high copy number.The adaptability,recovery performance,selective resolution of(S)-type isomers and the catalytic capacity of(1S,4S)-demethylsertraline were further evaluated.The results showed that the immobilized P-ω-TA retained its full activity and adaptability,with easy recovery through centrifugation for repeated uses.In a five-round recovery and re-use process,the recovery rate of enzyme activity was greater than 91％for each round.After five times of catalysis,the final enzyme activity retention rate was about 84％.The immobilized P-ω-TA maintained the(S)-type selective resolution at the chiral center of the substrate and the catalytic capacity of(1S,4S)-demethylsertraline.
Pseudovibrio-ω-transaminasebacteriophage T4chiral resolutionenzyme immobilizationsertralinefine chemical intermediates
万方数据
维普
