Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates
The main objective of this study is the enantioselective synthesis of carboxyhydroxyphosphonates by lipase-catalyzed reactions. For this purpose, racemic dimethyl and dibutyl 1-butyryloxy-1-carboxymethylphosphonates were synthesized and hydrolyzed, using a wide spectrum of commercially available lip...
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MDPI AG
2021-08-01
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| Online Access: | https://www.mdpi.com/2073-4344/11/8/956 |
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| author | Paulina Majewska |
| author_facet | Paulina Majewska |
| author_sort | Paulina Majewska |
| collection | DOAJ |
| description | The main objective of this study is the enantioselective synthesis of carboxyhydroxyphosphonates by lipase-catalyzed reactions. For this purpose, racemic dimethyl and dibutyl 1-butyryloxy-1-carboxymethylphosphonates were synthesized and hydrolyzed, using a wide spectrum of commercially available lipases from different sources (e.g., fungi and bacteria). The best hydrolysis results of dimethyl 1-butyryloxy-1-carboxymethylphosphonate were obtained with the use of lipases from <i>Candida rugosa</i>, <i>Candida antarctica</i>, and <i>Aspergillus niger</i>, leading to optically active dimethyl 1-carboxy-1-hydroxymethylphosphonate (58%–98% enantiomeric excess) with high enantiomeric ratio (reaching up to 126). However, in the case of hydrolysis of dibutyl 1-butyryloxy-1-carboxymethylphosphonate, the best results were obtained by lipases from <i>Burkholderia cepacia</i> and <i>Termomyces lanuginosus</i>, leading to optically active dibutyl 1-carboxy-1-hydroxymethylphosphonate (66%–68% enantiomeric excess) with moderate enantiomeric ratio (reaching up to 8.6). The absolute configuration of the products after biotransformation was also determined. In most cases, lipases hydrolyzed (<i>R</i>) enantiomers of both compounds. |
| first_indexed | 2024-03-10T08:56:38Z |
| format | Article |
| id | doaj.art-8720d5598912469a98a31e9d65e47332 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T08:56:38Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-8720d5598912469a98a31e9d65e473322023-11-22T07:07:15ZengMDPI AGCatalysts2073-43442021-08-0111895610.3390/catal11080956Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonatesPaulina Majewska0Laboratory of Biotechnology, Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, PolandThe main objective of this study is the enantioselective synthesis of carboxyhydroxyphosphonates by lipase-catalyzed reactions. For this purpose, racemic dimethyl and dibutyl 1-butyryloxy-1-carboxymethylphosphonates were synthesized and hydrolyzed, using a wide spectrum of commercially available lipases from different sources (e.g., fungi and bacteria). The best hydrolysis results of dimethyl 1-butyryloxy-1-carboxymethylphosphonate were obtained with the use of lipases from <i>Candida rugosa</i>, <i>Candida antarctica</i>, and <i>Aspergillus niger</i>, leading to optically active dimethyl 1-carboxy-1-hydroxymethylphosphonate (58%–98% enantiomeric excess) with high enantiomeric ratio (reaching up to 126). However, in the case of hydrolysis of dibutyl 1-butyryloxy-1-carboxymethylphosphonate, the best results were obtained by lipases from <i>Burkholderia cepacia</i> and <i>Termomyces lanuginosus</i>, leading to optically active dibutyl 1-carboxy-1-hydroxymethylphosphonate (66%–68% enantiomeric excess) with moderate enantiomeric ratio (reaching up to 8.6). The absolute configuration of the products after biotransformation was also determined. In most cases, lipases hydrolyzed (<i>R</i>) enantiomers of both compounds.https://www.mdpi.com/2073-4344/11/8/956biocatalysishydroxyphosphonateslipolytic activitydetermination of absolute configurationenantiomers |
| spellingShingle | Paulina Majewska Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates Catalysts biocatalysis hydroxyphosphonates lipolytic activity determination of absolute configuration enantiomers |
| title | Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates |
| title_full | Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates |
| title_fullStr | Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates |
| title_full_unstemmed | Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates |
| title_short | Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates |
| title_sort | lipase catalyzed kinetic resolution of dimethyl and dibutyl 1 butyryloxy 1 carboxymethylphosphonates |
| topic | biocatalysis hydroxyphosphonates lipolytic activity determination of absolute configuration enantiomers |
| url | https://www.mdpi.com/2073-4344/11/8/956 |
| work_keys_str_mv | AT paulinamajewska lipasecatalyzedkineticresolutionofdimethylanddibutyl1butyryloxy1carboxymethylphosphonates |