Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester
The present study was conducted to purify lipase from indigenous Bacillus subtilis strain Kakrayal_1 (BSK-L) for enantioselective resolution of racemic-ketoprofen. The production of lipase (BSK-L) was optimized using Plackett–Burman and central composite design of response surface methodology (RSM)....
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ftpubmed:oai:pubmedcentral.nih.gov:6242800 2023-05-15T13:33:55+02:00 Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester Saraswat, Rashmi Bhushan, Indu Gupta, Pankaj Kumar, Vivek Verma, Vijeshwar 2018-11-19 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242800/ http://www.ncbi.nlm.nih.gov/pubmed/30498664 https://doi.org/10.1007/s13205-018-1506-6 en eng Springer International Publishing http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242800/ http://www.ncbi.nlm.nih.gov/pubmed/30498664 http://dx.doi.org/10.1007/s13205-018-1506-6 © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Original Article Text 2018 ftpubmed https://doi.org/10.1007/s13205-018-1506-6 2019-12-08T01:15:37Z The present study was conducted to purify lipase from indigenous Bacillus subtilis strain Kakrayal_1 (BSK-L) for enantioselective resolution of racemic-ketoprofen. The production of lipase (BSK-L) was optimized using Plackett–Burman and central composite design of response surface methodology (RSM). The optimized media containing olive oil (3.5%), MnSO(4) (8 mM), CaCl(2) (5 mM), peptone (20 g/l), pH (8), agitation (180 rpm) and temperature (37 °C) resulted in maximum lipase production of 7500 U/g of cell biomass. The lipase was purified using sequential method to an overall purification fold of 13% with 20% recovery, 882 U/mg specific activity and a molecular weight of 45 kDa. Optimal pH and temperature of purified lipase were found to be 8 and 37 °C, respectively. Furthermore, BSK-L displayed good stability with various organic solvents, surfactants and metal ions. K(m) and V(max) values of lipase were observed to be 2.2 mM and 6.67 mmoles of product formed/min/mg, respectively. The racemic ketoprofen butyl ester was hydrolyzed using lipase with 49% conversion efficiency and 69% enantiomeric excess (ee) which was superior to the commercially procured lipase (Candida antarctica lipase). Thus, this enzyme could be considered as a promising candidate for the pharmaceutical industry. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13205-018-1506-6) contains supplementary material, which is available to authorized users. Text Antarc* Antarctica PubMed Central (PMC) 3 Biotech 8 12 |
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Original Article Saraswat, Rashmi Bhushan, Indu Gupta, Pankaj Kumar, Vivek Verma, Vijeshwar Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester |
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Original Article |
description |
The present study was conducted to purify lipase from indigenous Bacillus subtilis strain Kakrayal_1 (BSK-L) for enantioselective resolution of racemic-ketoprofen. The production of lipase (BSK-L) was optimized using Plackett–Burman and central composite design of response surface methodology (RSM). The optimized media containing olive oil (3.5%), MnSO(4) (8 mM), CaCl(2) (5 mM), peptone (20 g/l), pH (8), agitation (180 rpm) and temperature (37 °C) resulted in maximum lipase production of 7500 U/g of cell biomass. The lipase was purified using sequential method to an overall purification fold of 13% with 20% recovery, 882 U/mg specific activity and a molecular weight of 45 kDa. Optimal pH and temperature of purified lipase were found to be 8 and 37 °C, respectively. Furthermore, BSK-L displayed good stability with various organic solvents, surfactants and metal ions. K(m) and V(max) values of lipase were observed to be 2.2 mM and 6.67 mmoles of product formed/min/mg, respectively. The racemic ketoprofen butyl ester was hydrolyzed using lipase with 49% conversion efficiency and 69% enantiomeric excess (ee) which was superior to the commercially procured lipase (Candida antarctica lipase). Thus, this enzyme could be considered as a promising candidate for the pharmaceutical industry. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13205-018-1506-6) contains supplementary material, which is available to authorized users. |
format |
Text |
author |
Saraswat, Rashmi Bhushan, Indu Gupta, Pankaj Kumar, Vivek Verma, Vijeshwar |
author_facet |
Saraswat, Rashmi Bhushan, Indu Gupta, Pankaj Kumar, Vivek Verma, Vijeshwar |
author_sort |
Saraswat, Rashmi |
title |
Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester |
title_short |
Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester |
title_full |
Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester |
title_fullStr |
Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester |
title_full_unstemmed |
Production and purification of an alkaline lipase from Bacillus sp. for enantioselective resolution of (±)-Ketoprofen butyl ester |
title_sort |
production and purification of an alkaline lipase from bacillus sp. for enantioselective resolution of (±)-ketoprofen butyl ester |
publisher |
Springer International Publishing |
publishDate |
2018 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242800/ http://www.ncbi.nlm.nih.gov/pubmed/30498664 https://doi.org/10.1007/s13205-018-1506-6 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242800/ http://www.ncbi.nlm.nih.gov/pubmed/30498664 http://dx.doi.org/10.1007/s13205-018-1506-6 |
op_rights |
© Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
op_doi |
https://doi.org/10.1007/s13205-018-1506-6 |
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3 Biotech |
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8 |
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12 |
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1766046926568947712 |