Recognition of the remote chiral center in lipase-catalyzed kinetic resolution of [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate, the precursor of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid)

Naoki Natori, Kaoruko Nakagawara, Mitsuru Shoji, Takeshi Sugai, Kengo Hanaya

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

To access the enantiomers of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid), lipase-catalyzed kinetic resolution of racemic [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate was examined with Burkholderia cepacia lipase (Amano PS-IM) and Candida antarctica lipase B (Novozym 435) under transesterification conditions. Enantioselectivity of B. cepacia lipase (E = 72) was higher than that of C. antarctica lipase B (E = 1.7), and these lipases showed a reversal of enantiopreference in the recognition of a remote chiral center. The computational study showed that the tetrahedral intermediate complex of B. cepacia lipase with (R)-4a, the fast isomer, was more stable than that with (S)-4a, the slow isomer. The repetitive use of B. cepacia lipase and further chemical transformation provided both enantiomers [(R)-: 99.4% ee and (S)-: 99.4% ee] of MNB carboxylic acid as methyl esters.

Original languageEnglish
Pages (from-to)130-135
Number of pages6
JournalJournal of Molecular Catalysis B: Enzymatic
Volume109
DOIs
Publication statusPublished - 2014

Fingerprint

Enzyme kinetics
Lipases
Carboxylic Acids
Lipase
Carboxylic acids
Kinetics
Burkholderia cepacia
Enantiomers
Isomers
Burkholderia cepacia complex
Enantioselectivity
Transesterification
1,3-benzodioxole
methyl acetate
Candida
Esters

Keywords

  • Kinetic resolution
  • Lipase
  • Molecular dynamics simulation
  • Remote chiral center
  • Transesterification

ASJC Scopus subject areas

  • Biochemistry
  • Bioengineering
  • Catalysis
  • Process Chemistry and Technology

Cite this

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title = "Recognition of the remote chiral center in lipase-catalyzed kinetic resolution of [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate, the precursor of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid)",
abstract = "To access the enantiomers of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid), lipase-catalyzed kinetic resolution of racemic [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate was examined with Burkholderia cepacia lipase (Amano PS-IM) and Candida antarctica lipase B (Novozym 435) under transesterification conditions. Enantioselectivity of B. cepacia lipase (E = 72) was higher than that of C. antarctica lipase B (E = 1.7), and these lipases showed a reversal of enantiopreference in the recognition of a remote chiral center. The computational study showed that the tetrahedral intermediate complex of B. cepacia lipase with (R)-4a, the fast isomer, was more stable than that with (S)-4a, the slow isomer. The repetitive use of B. cepacia lipase and further chemical transformation provided both enantiomers [(R)-: 99.4{\%} ee and (S)-: 99.4{\%} ee] of MNB carboxylic acid as methyl esters.",
keywords = "Kinetic resolution, Lipase, Molecular dynamics simulation, Remote chiral center, Transesterification",
author = "Naoki Natori and Kaoruko Nakagawara and Mitsuru Shoji and Takeshi Sugai and Kengo Hanaya",
year = "2014",
doi = "10.1016/j.molcatb.2014.08.010",
language = "English",
volume = "109",
pages = "130--135",
journal = "Journal of Molecular Catalysis - B Enzymatic",
issn = "1381-1177",
publisher = "Elsevier",

}

TY - JOUR

T1 - Recognition of the remote chiral center in lipase-catalyzed kinetic resolution of [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate, the precursor of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid)

AU - Natori, Naoki

AU - Nakagawara, Kaoruko

AU - Shoji, Mitsuru

AU - Sugai, Takeshi

AU - Hanaya, Kengo

PY - 2014

Y1 - 2014

N2 - To access the enantiomers of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid), lipase-catalyzed kinetic resolution of racemic [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate was examined with Burkholderia cepacia lipase (Amano PS-IM) and Candida antarctica lipase B (Novozym 435) under transesterification conditions. Enantioselectivity of B. cepacia lipase (E = 72) was higher than that of C. antarctica lipase B (E = 1.7), and these lipases showed a reversal of enantiopreference in the recognition of a remote chiral center. The computational study showed that the tetrahedral intermediate complex of B. cepacia lipase with (R)-4a, the fast isomer, was more stable than that with (S)-4a, the slow isomer. The repetitive use of B. cepacia lipase and further chemical transformation provided both enantiomers [(R)-: 99.4% ee and (S)-: 99.4% ee] of MNB carboxylic acid as methyl esters.

AB - To access the enantiomers of 2-methyl-2-(2′-naphthyl)-1,3-benzodioxole-4-carboxylic acid (MNB carboxylic acid), lipase-catalyzed kinetic resolution of racemic [2-methyl-2-(2′-naphthyl)-1,3-benzodioxol-4-yl]methyl acetate was examined with Burkholderia cepacia lipase (Amano PS-IM) and Candida antarctica lipase B (Novozym 435) under transesterification conditions. Enantioselectivity of B. cepacia lipase (E = 72) was higher than that of C. antarctica lipase B (E = 1.7), and these lipases showed a reversal of enantiopreference in the recognition of a remote chiral center. The computational study showed that the tetrahedral intermediate complex of B. cepacia lipase with (R)-4a, the fast isomer, was more stable than that with (S)-4a, the slow isomer. The repetitive use of B. cepacia lipase and further chemical transformation provided both enantiomers [(R)-: 99.4% ee and (S)-: 99.4% ee] of MNB carboxylic acid as methyl esters.

KW - Kinetic resolution

KW - Lipase

KW - Molecular dynamics simulation

KW - Remote chiral center

KW - Transesterification

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JO - Journal of Molecular Catalysis - B Enzymatic

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