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Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration.
J Biotechnol 2017; 243:1-9JB

Abstract

Optically pure 1-phenyl-1,2-ethanediol is a very important chiral building block and intermediate in fine chemical and pharmaceutical industries. Reduction of 2-hydroxyacetophenone provides a straightforward approach to access these important compounds. In this study, two enantiocomplementary carbonyl reductases, BDHA (2,3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) were discovered for the first time to convert 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) and (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, respectively. The two enzymes were purified and characterized. In vitro bioreduction of 2-HAP catalyzed by BDHA and GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration were demonstrated, affording both (R)-PED and (S)-PED in>99% ee and 99% conversion. Recombinant Escherichia coli whole cells co-expressing both GDH and BDHA or GoSCR genes were used to asymmetric reduction of 2-HAP to (R)-PED or (S)-PED. Under the optimized conditions, the bioreduction of 400mM (54g/L) substrate was proceeded smoothly without the external addition of cofactor, and the product (R)-PED and (S)-PED were obtained with 99% yield, >99% ee and 18.0g/L/h volumetric productivity. These results offer a practical biocatalytic method for the preparation of both (R)-PED and (S)-PED with high volumetric productivity.

Authors+Show Affiliations

Department of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, Taiyuan, Shanxi, 030024, PR China.Department of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, Taiyuan, Shanxi, 030024, PR China. Electronic address: zhangjiandong@tyut.edu.cn.Department of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, Taiyuan, Shanxi, 030024, PR China.State Key Laboratory of Bioreactor Engineering, Shanghai Collaborative Innovation Center for Biomanufacture, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, PR China.Department of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, Taiyuan, Shanxi, 030024, PR China. Electronic address: changhonghong@tyut.edu.cn.Department of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, Taiyuan, Shanxi, 030024, PR China.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28011130

Citation

Cui, Zhi-Mei, et al. "Highly Efficient Bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol By Two Substrate Tolerance Carbonyl Reductases With Cofactor Regeneration." Journal of Biotechnology, vol. 243, 2017, pp. 1-9.
Cui ZM, Zhang JD, Fan XJ, et al. Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration. J Biotechnol. 2017;243:1-9.
Cui, Z. M., Zhang, J. D., Fan, X. J., Zheng, G. W., Chang, H. H., & Wei, W. L. (2017). Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration. Journal of Biotechnology, 243, pp. 1-9. doi:10.1016/j.jbiotec.2016.12.016.
Cui ZM, et al. Highly Efficient Bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol By Two Substrate Tolerance Carbonyl Reductases With Cofactor Regeneration. J Biotechnol. 2017 Feb 10;243:1-9. PubMed PMID: 28011130.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration. AU - Cui,Zhi-Mei, AU - Zhang,Jian-Dong, AU - Fan,Xiao-Jun, AU - Zheng,Gao-Wei, AU - Chang,Hong-Hong, AU - Wei,Wen-Long, Y1 - 2016/12/21/ PY - 2016/08/28/received PY - 2016/12/12/revised PY - 2016/12/19/accepted PY - 2016/12/25/pubmed PY - 2017/4/5/medline PY - 2016/12/25/entrez KW - 2-Hydroxyacetophenone KW - Carbonyl reductase KW - Chiral 1-phenyl-1,2-ethanediol KW - Cofactor regeneration KW - Highly enantioselective SP - 1 EP - 9 JF - Journal of biotechnology JO - J. Biotechnol. VL - 243 N2 - Optically pure 1-phenyl-1,2-ethanediol is a very important chiral building block and intermediate in fine chemical and pharmaceutical industries. Reduction of 2-hydroxyacetophenone provides a straightforward approach to access these important compounds. In this study, two enantiocomplementary carbonyl reductases, BDHA (2,3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) were discovered for the first time to convert 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) and (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, respectively. The two enzymes were purified and characterized. In vitro bioreduction of 2-HAP catalyzed by BDHA and GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration were demonstrated, affording both (R)-PED and (S)-PED in>99% ee and 99% conversion. Recombinant Escherichia coli whole cells co-expressing both GDH and BDHA or GoSCR genes were used to asymmetric reduction of 2-HAP to (R)-PED or (S)-PED. Under the optimized conditions, the bioreduction of 400mM (54g/L) substrate was proceeded smoothly without the external addition of cofactor, and the product (R)-PED and (S)-PED were obtained with 99% yield, >99% ee and 18.0g/L/h volumetric productivity. These results offer a practical biocatalytic method for the preparation of both (R)-PED and (S)-PED with high volumetric productivity. SN - 1873-4863 UR - https://www.unboundmedicine.com/medline/citation/28011130/Highly_efficient_bioreduction_of_2_hydroxyacetophenone_to__S___and__R__1_phenyl_12_ethanediol_by_two_substrate_tolerance_carbonyl_reductases_with_cofactor_regeneration_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0168-1656(16)31663-7 DB - PRIME DP - Unbound Medicine ER -