Skip to main content
SpringerLink
Log in

Chromobacterium viscosum lipase catalyzes the transesterifications at the carboxyl site as well as the hydroxy site during the enzymatic enantioselective alcoholysis of O-acylated mandelates

  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

During the enzyme-catalyzed deacylation of O-acylated mandelates with an alcohol, Chromobacterium viscosum lipase was found to catalyze the transesterifications not only at the hydroxy site but also at the carboxyl site of mandelic acids, while such a side-reaction at the carboxyl site was negligible with the other lipases examined.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Akita H, Matsukura H, Oishi T (1986) Lipase catalyzed enantioselective hydrolysis of 2-methyl 3-acetoxy esters. Tetrahedron Lett. 27: 5241–5244.

    Google Scholar 

  • Chen C-S, Fujimoto Y, Girdaukas G, Sih CJ (1982) Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 104: 7294–7299.

    Google Scholar 

  • Chênevert R, Létourneau M (1990) Enantioselectivity of carbonic anhydrase catalyzed hydrolysis of mandelic methyl esters. Can. J. Chem. 68: 314–316.

    Google Scholar 

  • Coppola GM, Schuster HF (1997) α-Hydroxy Acids in Enantioselective Syntheses, Weinheim: VCH, pp. 137–165.

    Google Scholar 

  • Feichter C, Faber K, Griengl H (1989) Biocatalytic resolution of long-chain 3-hydroxyalkanoic esters. Tetrahedron Lett. 30: 551–552.

    Google Scholar 

  • Miyazawa T, Kurita S, Ueji S, Yamada T (1999a) Resolution of mandelic acids by lipase-catalyzed transesterifications in organic media. Biocatal. Biotrans. 16: in press.

  • Miyazawa T, Shimaoka M, Yamada T (1999b) Resolution of 2-cyano-2-methylalkanoic acids via porcine pancreatic lipase-catalyzed enantioselective ester hydrolysis: effect of the alcohol moiety of the substrate ester on enantioselectivity. Biotechnol. Lett. 21: 309–312.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Chemistry, Faculty of Science, Konan University, Higashinada-ku, Kobe, 658-8501, Japan

    Toshifumi Miyazawa, Sota Kurita & Takashi Yamada

  2. Division of Natural Environment and Bioorganic Chemistry, Faculty of Human Development and Sciences, Kobe University, Nada-ku, Kobe, 657-8501, Japan

    Shinichi Ueji

Authors
  1. Toshifumi Miyazawa
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Sota Kurita
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Shinichi Ueji
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Takashi Yamada
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Miyazawa, T., Kurita, S., Ueji, S. et al. Chromobacterium viscosum lipase catalyzes the transesterifications at the carboxyl site as well as the hydroxy site during the enzymatic enantioselective alcoholysis of O-acylated mandelates. Biotechnology Letters 21, 1023–1027 (1999). https://doi.org/10.1023/A:1005650600997

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005650600997

Search

Navigation