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Journal of Dairy Science Vol. 82 No. 3 466-471
© 1999 by American Dairy Science Association ®
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Measurement of Bile Salt Hydrolase Activity from Lactobacillus acidophilus Based on Disappearance of Conjugated Bile Salts

G. Corzo 1 and S. E. Gilliland 1

1 Department of Animal Science, Oklahoma State University, Stillwater 74078

Bile salt hydrolase activity of Lactobacillus acidophilus was measured based on the disappearance of sodium glycocholate and sodium taurocholate from the reaction mixture using HPLC. The amount of sodium glycocholate and sodium taurocholate that disappeared was proportional to the amount of sodium cholate that appeared in the mixture as detected by HPLC. Sodium glycocholate did not precipitate at the enzyme reaction conditions (37°C and pH 5.4) for determining bile salt hydrolase activity. The bile salt hydrolase assay was insensitive to low oxidation-reduction potential when measuring bile salt hydrolase from L. acidophilus, an intestinal microorganism. However, EDTA and freezing temperatures were necessary to maintain stability of the partially purified enzyme during storage.

Key Words: bile salt hydrolase • Lactobacillus acidophilus • sodium taurocholate • sodium glycocholate

Submitted on June 19, 1998
Accepted on November 16, 1998




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