Enantioselective resolution of (+/-)-1-phenylethyl acetate by extracellular proteases from deep-sea bacterium Bacillus sp. DL-2 | |
Hu, Yunfeng2,4; Sun, Aijun1; Zhang, Yun1; Xu, Yongkai3; Dong, Lu1,2 | |
刊名 | BIOCATALYSIS AND BIOTRANSFORMATION |
关键词 | Asymmetric hydrolysis extracellular proteases immobilization marine microorganisms (R)-1-phenylethanol (S)-1-phenylethyl acetate |
ISSN号 | 1024-2422 |
DOI | 10.1080/10242422.2019.1616697 |
英文摘要 | Chiral 1-phenylethanol and its ester derivative are important chiral chemicals in diverse industries and the preparation of those optically pure enantiomers is of great importance. One bacterium, Bacillus sp. DL-2, whose extracellular proteases could efficiently asymmetrically hydrolyse (+/-)-1-phenylethyl acetate, was isolated from the deep sea of the Western Pacific. After the immobilization of extracellular proteases and the optimization of enzymatic reactions, (R)-1-phenylethanol was prepared with the enantiomeric excess (e.e.) being 97% and the yield being 41%, respectively. The optimal resolution reaction condition for the preparation of (R)-1-phenylethanol using immobilized extracellular proteases was found to be 5-mM (+/-)-1-phenylethyl acetate, 360 mg/mL immobilized extracellular proteases, pH 6.5, and 20 degrees C for 2 h. (S)-1-phenylethyl acetate was generated through enzymatic kinetic resolution with the e.e. being as high as 99% and the yield being 71%, respectively. The optimal resolution reaction condition for the preparation of (S)-1-phenylethyl acetate was found to be 2.5-mM (+/-)-1-phenylethyl acetate, 440 mg/mL immobilized extracellular proteases, pH 7.5, and 35 degrees C for 10 h. Our report is the first report about the kinetic resolution of (+/-)-1-phenylethyl acetate using proteases and the enantio-preference of the proteases was found to be the same as those of most other esterases/lipases. Also notably, the optical purity of (S)-1-phenylethyl acetate generated through kinetic resolution using the proteases of Bacillus sp. DL-2 was the highest report so far. Proteases from deep-sea Bacillus sp. DL-2 are new contributions to the biocatalyst library for the preparation of valuable chiral alcohols and chiral esters through kinetic resolution. |
内容类型 | 期刊论文 |
源URL | [http://ir.scsio.ac.cn/handle/344004/17842] |
专题 | 南海海洋研究所_中科院海洋生物资源可持续利用重点实验室 |
作者单位 | 1.Univ Chinese Acad Sci, Beijing, Peoples R China 2.Chinese Acad Sci, South China Sea Inst Oceanol, CAS Key Lab Trop Marine Bioresources & Ecol, Guangzhou, Guangdong, Peoples R China 3.Chinese Acad Sci, South China Sea Inst Oceanol, Guangdong Key Lab Marine Mat Med, Guangzhou, Guangdong, Peoples R China 4.Shandong Univ Tradit Chinese Med, Affiliated Hosp, Jinan, Shandong, Peoples R China 5.South China Sea Bioresource Exploitat & Utilizat, Guangzhou, Guangdong, Peoples R China |
推荐引用方式 GB/T 7714 | Hu, Yunfeng,Sun, Aijun,Zhang, Yun,et al. Enantioselective resolution of (+/-)-1-phenylethyl acetate by extracellular proteases from deep-sea bacterium Bacillus sp. DL-2[J]. BIOCATALYSIS AND BIOTRANSFORMATION. |
APA | Hu, Yunfeng,Sun, Aijun,Zhang, Yun,Xu, Yongkai,&Dong, Lu. |
MLA | Hu, Yunfeng,et al."Enantioselective resolution of (+/-)-1-phenylethyl acetate by extracellular proteases from deep-sea bacterium Bacillus sp. DL-2".BIOCATALYSIS AND BIOTRANSFORMATION |
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