SpringerLink
Log in

Mandelate racemase assayed by polarimetry

  • Published:
Biotechnology Techniques

Abstract

An accurate and convenient assay for mandelate racemase based on polarimetry was developed by making use of the time-dependent decrease of the optical rotation of the substrate (D- or L-mandelate) at 589 nm (Na-D-line) during the enzyme-catalyzed racemization. In comparison to the indirect assay methods hitherto used, this method has the following advantages: (i) it is faster and more accurate than the two-enzyme redox assay (which needs a membrane-bound protein fraction), (ii) it is also applicable to non-natural substrates other than mandelate, provided their specific optical rotation is large enough and (iii) it does not rely on expensive equipment such as circular dicroism. © Rapid Science Ltd. 1998

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

Access this article

Log in via an institution

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price includes VAT (United Kingdom)

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Adams, E (1976). Adv. Enzymol. Relat. Areas Mol. Biol. 44: 69-138

    Google Scholar 

  • Armstrong, JM (1964). Biochim. Biophys. Acta 86: 194-197

    Google Scholar 

  • Cardinale, GJ and Abeles, RH (1968). Biochemistry 7: 3970-3978

    Google Scholar 

  • Fee, JA, Hegeman, GD and Kenyon, GL (1974). Biochemistry 12: 2528-2532

    Google Scholar 

  • Finlay, TH and Adams, E (1970). J. Biol. Chem. 245: 5248-5260

    Google Scholar 

  • Hegeman, GD (1966). J. Bacteriol. 91: 1140-1154

    Google Scholar 

  • Hegeman, GD (1970). Methods Enzymol. 17: 670-673

    Google Scholar 

  • Hegeman, GD, Rosenberg, EY and Kenyon, GL (1970). Biochemistry 9: 4029-4035

    Google Scholar 

  • Kagan, HB, Girard, C, Guillaneux, D, Rainford, D, Samuel, O, Zhang, SY and Zhao, SH (1996). Acta Chem. Scand. 50: 345-352

    Google Scholar 

  • Kenyon, GL and Hegeman, GD (1979). Adv. Enzymol. Relat. Areas Mol. Biol. 50: 325-360

    Google Scholar 

  • Kenyon, GL, Gerlt, JA, Petsko, GA and Kozarich, JW (1995). Acc. Chem. Res. 28: 178-186

    Google Scholar 

  • Landro, JA, Kenyon, GL and Kozarich, JW (1992). Bioorg. Med. Chem. Lett. 2: 1411-1418

    Google Scholar 

  • Li, R, Powers, VM, Kozarich, JW and Kenyon, GL (1995). J. Org. Chem. 60: 3347-3351

    Google Scholar 

  • McClure, WR (1969). Biochemistry 8: 2782-2786

    Google Scholar 

  • Petsko, GA, Kenyon, GL, Gerlt, JA, Ringe, D and Kozarich, JW (1993). Trends Biochem. Sci. 18: 372-376

    Google Scholar 

  • Sharp, TR, Hegeman, GD and Kenyon, GL (1979). Anal. Biochem. 94: 329-334

    Google Scholar 

  • Stecher, H and Faber, K (1997). Synthesis 1-16

  • Stecher, H, Felfer, U and Faber, K. (1997). J. Biotechnol. 56: 33-40

    Google Scholar 

  • Weil-Malherbe, H (1966). Biochem. J. 101: 169-175

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Organic Chemistry, Institute of Biochemistry, Graz University of Technology, Stremayrgasse, Graz, Austria

    Hartmut Stecher, Albin Hermetter & Kurt Faber

Authors
  1. Hartmut Stecher
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Albin Hermetter
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Kurt Faber
    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

Stecher, H., Hermetter, A. & Faber, K. Mandelate racemase assayed by polarimetry. Biotechnology Techniques 12, 257–261 (1998). https://doi.org/10.1023/A:1008837911630

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1008837911630

Keywords

Search

Navigation