Lipase-catalysed enantioselective kinetic resolution of rac-lipidic alkynylcarbinols and a C5 synthon thereof via a hydrolysis approach

Autor: Yves Génisson, Marcos Reinaldo da Silva, Stéphanie Ballereau, Remi Chauvin, Marcos Carlos de Mattos, Maria da Conceição F. de Oliveira, Valérie Maraval, Fátima M. Nunes, Diana Kelly Castro de Almeida
Přispěvatelé: Laboratory of Biotechnology and Organic Synthesis, Federal University of Ceara, Universidade Federal do Ceará = Federal University of Ceará (UFC), Synthèse et Physico-Chimie de Molécules d'Intérêt Biologique (SPCMIB), Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de chimie de coordination (LCC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), CAPES-COFECUB program, Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Zdroj: Molecular Catalysis
Molecular Catalysis, Elsevier, 2020, 488, pp.110926. ⟨10.1016/j.mcat.2020.110926⟩
Molecular Catalysis, 2020, 488, pp.110926. ⟨10.1016/j.mcat.2020.110926⟩
ISSN: 2468-8231
DOI: 10.1016/j.mcat.2020.110926⟩
Popis: International audience; Lipase-mediated kinetic resolution (LMKR) of three racemic lipidic alkynylcarbinol (LAC) acetates, rac-heptadeca-1,4-diyn-3-yl acetate (rac-2-Ac), rac-heptadeca-1,4,6-triyn-3-yl acetate (rac-3-Ac) and rac-heptadeca-1-yn-3yl acetate (rac-4-Ac), besides the versatile C5 synthon dialkynylcarbinol (DAC) acetate, rac-(triisopropylsilyl)penta-1,4-diyn-3-yl acetate (rac-5), was studied. CAL-B immobilized on acrylic resin was investigated as catalyst on LMKR of rac-2-5-Ac. Fourteen commercial lipases (immobilized and free forms), besides one esterase, were also investigated on the LMKR of rac-5-Ac. After investigation of reaction parameters, optimal conditions were established for each compound, yielding both (R)- and (S)-alcohols in 50 % conversions, enantioselectivities (E) >200 and high e.e. values [(R)-2 and (S)-2-Ac, e.e. >99 %; (R)-3 and (S)-3-Ac, e.e. 98 %; (R)-4 and (S)-4-Ac, e.e. 96 %; (R)-5 and (S)-5-Ac, e.e. >99 %]. Except for rac-5-Ac that had Thermomyces lanuginosus immobilized on immobead-150 as best catalyst, CAL-B was the most efficient lipase on LMKR of rac-2-4-Ac. (S)-Alcohols were obtained by lipase-mediated hydrolysis of (S)-acetate compounds, using CAL-B for (S)-4-Ac (57.5 % yield and e.e. 96 %) and lipase from Candida rugosa for (S)-5-Ac (53 % yield and e.e. >99 %).
Databáze: OpenAIRE
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