Effect of imprinting sol-gel immobilized lipase with chiral template substrates in esterification of (R)-(+)- and (S)-(-)-glycidol

Shin Ya Furukawa, Tsutomu Ono, Hiroyuki Ijima, Koei Kawakami

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

To prepare an immobilized lipase effective for enantioselective esterification of glycidol with n-butyric acid in organic media, hybrid gel-entrapped lipase on Celite was prepared by the sol-gel method and pretreated with chiral template substrates. When n-butyltrimethoxysilane, (n-BuTrMOS) as an organic silane precursor, was mixed with tetramethoxysilane (TMOS) at a molar ratio of 4:1, the hybrid gel-entrapped lipase on Celite showed three times higher activity than the deposited lipase on Celite as a control. The pretreatment of this immobilized lipase with a hydrophobic enantiomer such as (R)-(-)-2-octanol brought about a selective enhancement of the activity for the esterification of (R)-(+)-glycidol, whereas such pretreatment hardly affected the activity for the esterification of (S)-(-)-glycidol. Consequently, the relative initial enantiomeric activity (RIEA) of the hybrid gel-entrapped lipase on Celite, defined as a ratio of the initial esterification rate of (R)-(+)-glycidol to that of (S)-(-)-glycidol, changed between 0.76 and 2.0. In addition, increasing the concentration of (R)-(-)-2-octanol as a template substrate, increased the activity and RIEA, and showed maximum values with the addition of 21mM of (R)-(-)-2-octanol.

Original languageEnglish
Pages (from-to)23-28
Number of pages6
JournalJournal of Molecular Catalysis B: Enzymatic
Volume17
Issue number1
DOIs
Publication statusPublished - Mar 7 2002
Externally publishedYes

Fingerprint

glycidol
Esterification
Lipases
Polymethyl Methacrylate
Lipase
Diatomaceous Earth
Sol-gels
Gels
Substrates
Silanes
Butyric acid
Butyric Acid
Enantiomers
Sol-gel process

Keywords

  • Enantioselective esterification
  • Imprinting
  • Lipase
  • Organic-inorganic hybrid silicate
  • Sol-gel method

ASJC Scopus subject areas

  • Biochemistry
  • Catalysis
  • Process Chemistry and Technology

Cite this

Effect of imprinting sol-gel immobilized lipase with chiral template substrates in esterification of (R)-(+)- and (S)-(-)-glycidol. / Furukawa, Shin Ya; Ono, Tsutomu; Ijima, Hiroyuki; Kawakami, Koei.

In: Journal of Molecular Catalysis B: Enzymatic, Vol. 17, No. 1, 07.03.2002, p. 23-28.

Research output: Contribution to journalArticle

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N2 - To prepare an immobilized lipase effective for enantioselective esterification of glycidol with n-butyric acid in organic media, hybrid gel-entrapped lipase on Celite was prepared by the sol-gel method and pretreated with chiral template substrates. When n-butyltrimethoxysilane, (n-BuTrMOS) as an organic silane precursor, was mixed with tetramethoxysilane (TMOS) at a molar ratio of 4:1, the hybrid gel-entrapped lipase on Celite showed three times higher activity than the deposited lipase on Celite as a control. The pretreatment of this immobilized lipase with a hydrophobic enantiomer such as (R)-(-)-2-octanol brought about a selective enhancement of the activity for the esterification of (R)-(+)-glycidol, whereas such pretreatment hardly affected the activity for the esterification of (S)-(-)-glycidol. Consequently, the relative initial enantiomeric activity (RIEA) of the hybrid gel-entrapped lipase on Celite, defined as a ratio of the initial esterification rate of (R)-(+)-glycidol to that of (S)-(-)-glycidol, changed between 0.76 and 2.0. In addition, increasing the concentration of (R)-(-)-2-octanol as a template substrate, increased the activity and RIEA, and showed maximum values with the addition of 21mM of (R)-(-)-2-octanol.

AB - To prepare an immobilized lipase effective for enantioselective esterification of glycidol with n-butyric acid in organic media, hybrid gel-entrapped lipase on Celite was prepared by the sol-gel method and pretreated with chiral template substrates. When n-butyltrimethoxysilane, (n-BuTrMOS) as an organic silane precursor, was mixed with tetramethoxysilane (TMOS) at a molar ratio of 4:1, the hybrid gel-entrapped lipase on Celite showed three times higher activity than the deposited lipase on Celite as a control. The pretreatment of this immobilized lipase with a hydrophobic enantiomer such as (R)-(-)-2-octanol brought about a selective enhancement of the activity for the esterification of (R)-(+)-glycidol, whereas such pretreatment hardly affected the activity for the esterification of (S)-(-)-glycidol. Consequently, the relative initial enantiomeric activity (RIEA) of the hybrid gel-entrapped lipase on Celite, defined as a ratio of the initial esterification rate of (R)-(+)-glycidol to that of (S)-(-)-glycidol, changed between 0.76 and 2.0. In addition, increasing the concentration of (R)-(-)-2-octanol as a template substrate, increased the activity and RIEA, and showed maximum values with the addition of 21mM of (R)-(-)-2-octanol.

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