Open AccessEnantioselective Resolution of (R,S)-Carvedilol to (S)-(−)-Carvedilol by Biocatalysts
Author(s) -
Ettireddy Swetha,
Vijitha Chandupatla,
Ciddi Veeresham
Publication year - 2017
Publication title -
natural products and bioprospecting
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.633
H-Index - 21
eISSN - 2192-2195
pISSN - 2192-2209
DOI - 10.1007/s13659-016-0118-2
Subject(s) - carvedilol , enantioselective synthesis , plant biochemistry , bioorganic chemistry , resolution (logic) , chemistry , biochemical engineering , computer science , catalysis , organic chemistry , medicine , engineering , biochemistry , artificial intelligence , enzyme , heart failure , gene
Among the microorganisms employed in the study, Aspergillus niger (GUFCC5443), Escherichia coli (ATCC9637), Streptomyces halstedii (CKM-2), Pseudomonas putida (NCIB9494), Cunninghamella elegans (NCIM689) and Sphingomonas paucimobilis (NCTC11030) were capable for the enantioselective conversion of racemic Carvedilol. Immobilization technique enhanced the enantioselectivity of microorganisms and thus increased the enantiomeric purity of the drug. Excellent enantiomeric ratios (E) were found in reactions catalyzed by immobilized A. niger and E. coli with values 174.44 and 104.26, respectively. Triacylglycerol lipase from Aspergillus niger was also employed in this study as a biocatalyst which resulted in the product with 83.35% enantiomeric excess (ee) and E of 11.34 while the enzyme on immobilization has yielded 99.08% ee and 216.39 E. The conversion yield (C%) of the drug by free-enzyme was 57.42%, which was enhanced by immobilization to 90.51%. Hence, our results suggest that immobilized triacylglycerol lipase from A. niger (Lipase AP6) could be an efficient biocatalyst for the enantioselective resolution of racemic Carvedilol to (S)-(-)-Carvedilol with high enantiomeric purity followed by immobilized cultures of A. niger and E. coli.