Skip to main content
SpringerLink
Log in

Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri

  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

The bile salt hydrolase (BSH) of Lactobacillus reuteri CRL 1098 is a single, constitutive, intracellular enzyme which is only detectable in stationary phase cells. It has optimal activity at pH 4.5–5.5 and 37–45 °C. The enzyme (80 kDa apparent mass) has sulphydryl groups in the catalytic active site and hydrolyzes both glycine and taurine conjugated bile acids with higher affinity for glyco-conjugates.

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

  • Church FC, David HP, Catagnani GL, Swaisgood HG (1985) An o-phthalaldehyde spectrophotometric assay for proteinases. Anal. Biochem. 146: 343–348.

    Google Scholar 

  • Coleman JP, Hudson LL (1995) Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens. Appl. Environ. Microbiol. 61: 2518–2520.

    Google Scholar 

  • De Man JCA, Rogosa M, Sharpe ME (1960) A medium for the cultivation of lactobacilli. J. Appl. Bacteriol. 23: 130–135.

    Google Scholar 

  • Dobrogosz WJ, Casas IA, Pagano GA, Talarico TL, Sjorberg B, Karlson M (1989) Lactobacillus reuteri and the enteric microbiota. In: Grubb R, Midtveldt T, Norin E, eds. The Regulatory and Protective Role of the Normal Microflora. London: Macmillan Ltd, pp. 69–96.

    Google Scholar 

  • Hylemon PB, Steilwag EJ (1976) Bile acid biotransformation rates from selected gram-positive and gram-negative intestinal anaerobic bacteria. Biochem. Biophys. Res. Commun. 69: 1088–1094.

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227: 680–685.

    Google Scholar 

  • Lundeen SG, Savage DC (1990). Characterization and purification of bile salt hydrolase fromLactobacillus sp. strain 100–100. J. Bacteriol. 172: 4171–4177.

    Google Scholar 

  • Taranto MP, Gonzalez de Llano D, Rodriguez A, Ruiz Holgado AP, Valdez GF (1996) Bile tolerance and cholesterol reduction by Enterococcus faecium, a candidate microorganism for the use as dietary adjunct. Milchwissenschaft. 51: 383–385.

    Google Scholar 

  • Taranto MP, Sesma F, Ruiz Holgado AP, Valdez GF (1997) Bile salts hydrolase plays a key role on cholesterol removal by Lactobacillus reuteri. Biotechnol. Lett. 19: 845–847.

    Google Scholar 

  • Taranto MP, Medici M, Perdigón G, Ruiz Holgado AP, Valdez GF (1998) Evidence of hypocholesterolemic effect of Lactobacillus reuteri in hypercholesterolemic mice. J. Dairy Sci. 81: 2336–2340.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Centro de Referencia para Lactobacilos (CERELA), CONICET, Chacabuco 145, 4000-, S.M. de Tucumán

    M.P. Taranto, F. Sesma & G. Font de Valdez

Authors
  1. M.P. Taranto
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. F. Sesma
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. G. Font de Valdez
    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

Taranto, M., Sesma, F. & Font de Valdez, G. Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri . Biotechnology Letters 21, 935–938 (1999). https://doi.org/10.1023/A:1005652501404

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005652501404

Search

Navigation