固定化c-ω-转氨酶催化合成(4S)-四氢萘酮  

Synthesis of(4S)-tetrahydronaphthalone catalyzed by immobilized Pseudovibrio-ω-aminotransferase

作　　者：高嵩 邵小芙 果波 李前 王佩[2] 曹阳 GAO Song;SHAO Xiaofu;GUO Bo;LI Qian;WANG Pei;CAO Yang(Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening,Jiangsu Ocean University,Lianyungang 222005,Jiangsu,China;School of Food Science and Pharmaceutical Engineering,Nanjing Normal University,Nanjing 210023,Jiangsu,China)

机构地区：[1]江苏海洋大学江苏省海洋药物活性分子筛选重点实验室,江苏连云港222005 [2]南京师范大学食品与制药工程学院,江苏南京210023

出　　处：《精细化工》2024年第5期1152-1160,共9页Fine Chemicals

基　　金：江苏省研究生科研与实践创新计划项目(KYCX2022-31)。

摘　　要：以T4噬菌体衣壳为载体,探索了海绵假弧菌-ω-转氨酶(P-ω-TA)的自组装固定化,以将P-ω-TA与T4噬菌体非必需小外壳蛋白(Soc)融合的方式实现了P-ω-TA在T4噬菌体衣壳上的亲和固定及较高的位点结合数。对固定化P-ω-TA的适应性、回收性能、(S)-型异构体选择性拆分及(1S,4S)-去甲基舍曲林的催化能力进行了测试。结果表明,固定化的P-ω-TA保持了完整的活性及适应性,可通过离心操作轻松地回收,并进行重复使用。在5次回收和重复使用过程中,每次酶活回收率均>91%,经5次催化,最终酶活保持率约为84%。固定化P-ω-TA保持了在底物手性中心处的(S)-型异构体选择性拆分以及对(1S,4S)-去甲基舍曲林的催化能力。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.

关 键 词：海绵假弧菌-ω-转氨酶 T4噬菌体 手性拆分 酶固定化 舍曲林 精细化工中间体 

分 类 号：TQ463[化学工程—制药化工] Q814.2[生物学—生物工程]