scholarly journals Bile Salt Hydrolase Activity and Resistance to Toxicity of Conjugated Bile Salts Are Unrelated Properties in Lactobacilli

2001 ◽  
Vol 67 (8) ◽  
pp. 3476-3480 ◽  
Author(s):  
Scott A. Moser ◽  
Dwayne C. Savage

ABSTRACT Bacteria of numerous species isolated from the human gastrointestinal tract express bile salt hydrolase (BSH) activity. How this activity contributes to functions of the microorganisms in the gastrointestinal tract is not known. We tested the hypothesis that a BSH protects the cells that produce it from the toxicity of conjugated bile salts. Forty-nine strains of numerous Lactobacillusspp. were assayed to determine their capacities to express BSH activities (taurodeoxycholic acid [TDCA] hydrolase and taurocholic acid [TCA] hydrolase activities) and their capacities to resist the toxicity of a conjugated bile acid (TDCA). Thirty of these strains had been isolated from the human intestine, 15 had been recovered from dairy products, and 4 had originated from other sources. Twenty-six of the strains expressed both TDCA hydrolase and TCA hydrolase activities. One strain that expressed TDCA hydrolase activity did not express TCA hydrolase activity. Conversely, in one strain for which the assay for TDCA hydrolase activity gave a negative result there was evidence of TCA hydrolase activity. Twenty-five of the strains were found to resist the toxicity of TDCA. Fourteen of these strains were of human origin, nine were from dairy products, and two were from other sources. Of the 26 strains expressing both TDCA hydrolase and TCA hydrolase activities, 15 were resistant to TDCA toxicity, 6 were susceptible, and 5 gave inconclusive results. Of the 17 strains that gave negative results for either of the enzymes, 7 were resistant to the toxicity, 9 were susceptible, and 1 gave inconclusive results. These findings do not support the hypothesis tested. They suggest, however, that BSH activity is important at some level for lactobacillus colonization of the human intestine.

2013 ◽  
Vol 781-784 ◽  
pp. 1336-1340
Author(s):  
Hui Liu ◽  
Yuan Hong Xie ◽  
Tao Han ◽  
Hong Xing Zhang

Cholesterol-lowering strains were obtained by high throughput screening technology and ortho-phthalaldehyde method. We used oxford cup method to screen again to obtain strains of high yield bile salt hydrolase and illuminate action mechanism ofLactobacillusreducing cholesterol. Screened six strains had the ability of high yield bile salt hydrolase and good ferment ability. The results of identifying bacteria species: strain KTxKL1J1 wereLactobacillus casei, strain Tx wasStreptococcus thermophilus, strain KS4P1 wereLactococcus lactis subsp.lactis, where the last two bacteria were strain of high yield bile salt hydrolase to be few known in literature. This work showed that dissociation bile salts and cholesterol conjuncted sediments by bile salt hydrolase decomposing conjugated bile salts.


2008 ◽  
Vol 74 (15) ◽  
pp. 4719-4726 ◽  
Author(s):  
Jolanda M. Lambert ◽  
Roger S. Bongers ◽  
Willem M. de Vos ◽  
Michiel Kleerebezem

ABSTRACT Bile salts play an important role in the digestion of lipids in vertebrates and are synthesized and conjugated to either glycine or taurine in the liver. Following secretion of bile salts into the small intestine, intestinal microbes are capable of deconjugating the glycine or taurine from the bile salts, using an enzyme called bile salt hydrolase (Bsh). Intestinal lactobacilli are regarded as major contributors to bile salt hydrolysis in vivo. Since the bile salt-hydrolyzing strain Lactobacillus plantarum WCFS1 was predicted to carry four bsh genes (bsh1, bsh2, bsh3, and bsh4), the functionality of these bsh genes was explored using Lactococcus lactis heterologous overexpression and multiple bsh deletion strains. Thus, Bsh1 was shown to be responsible for the majority of Bsh activity in L. plantarum WCFS1. In addition, bsh1 of L. plantarum WCFS1 was shown to be involved in conferring tolerance to specific bile salts (i.e., glycocholic acid). Northern blot analysis established that bsh1, bsh2, bsh3, and bsh4 are all expressed in L. plantarum WCFS1 during the exponential growth phase. Following biodiversity analysis, bsh1 appeared to be the only bsh homologue that was variable among L. plantarum strains; furthermore, the presence of bsh1 correlated with the presence of Bsh activity, suggesting that Bsh1 is commonly responsible for Bsh activity in L. plantarum strains. The fact that bsh2, bsh3, and bsh4 genes appeared to be conserved among L. plantarum strains suggests an important role of these genes in the physiology and lifestyle of the species L. plantarum. Analysis of these additional bsh-like genes in L. plantarum WCFS1 suggests that they might encode penicillin acylase rather than Bsh activity, indicating their implication in the conversion of substrates other than bile acids in the natural habitat.


1995 ◽  
Vol 108 (4) ◽  
pp. A928
Author(s):  
G. Thornton ◽  
M. O'Sullivan ◽  
G. O'Sullivan ◽  
A. Weerkamp ◽  
F. Shanahan ◽  
...  

2000 ◽  
Vol 46 (10) ◽  
pp. 878-884 ◽  
Author(s):  
J P Grill ◽  
S Perrin ◽  
F Schneider

The purpose of this work was to study some aspects of bile salt toxicity towards bifidobacteria. A strain (Bifidobacterium coryneforme ATCC 25911) was selected for its lack of conjugated bile salt hydrolase activity (CBSH-), and was used with three deconjugating strains (CBSH+), for study of their growth and viability in the presence of two dihydroxylated conjugated bile salts (tauro- and glyco-deoxycholic acids). The presence of the glycoconjugate induced a more significant growth inhibition for the four strains than the tauroconjugate. The viability of the strains was measured at several pH levels. Glycodeoxycholic acid, but not taurodeoxycholic acid, exerted a lethal effect, which increased at low pH. This phenomenon was more pronounced for the CBSH-strain. We explain some of these results using an hypothesis based on the consequence of dissociation of conjugated and deconjugated bile salts, and the value of their pKa.Key words: Bifidobacterium, viability, bile salt, deconjugation.


2002 ◽  
Vol 68 (6) ◽  
pp. 3126-3128 ◽  
Author(s):  
Mariangela Dean ◽  
Carlo Cervellati ◽  
Elena Casanova ◽  
Monica Squerzanti ◽  
Vincenzo Lanzara ◽  
...  

ABSTRACT Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60°C for up to 60 min, in agreement with calorimetric data.


Foods ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 674
Author(s):  
Jimmy G. Hernández-Gómez ◽  
Argelia López-Bonilla ◽  
Gabriela Trejo-Tapia ◽  
Sandra V. Ávila-Reyes ◽  
Antonio R. Jiménez-Aparicio ◽  
...  

Bile salt hydrolase (BSH) activity in probiotic strains is usually correlated with the ability to lower serum cholesterol levels in hypercholesterolemic patients. The objective of this study was the evaluation of BSH in five probiotic strains of lactic acid bacteria (LAB) and a probiotic yeast. The activity was assessed using a qualitative direct plate test and a quantitative high-performance thin- layer chromatography assay. The six strains differed in their BSH substrate preference and activity. Lactobacillus plantarum DGIA1, a potentially probiotic strain isolated from a double cream cheese from Chiapas, Mexico, showed excellent deconjugation activities in the four tested bile acids (69, 100, 81, and 92% for sodium glycocholate, glycodeoxycholate, taurocholate, and taurodeoxycholate, respectively). In the case of the commercial probiotic yeast Saccharomyces boulardii, the deconjugation activities were good against sodium glycodeoxycholate, taurocholate, and taurodeoxycholate (100, 57, and 63%, respectively). These last two results are part of the novelty of the work. A weak deconjugative activity (5%) was observed in the case of sodium glycocholate. This is the first time that the BSH activity has been detected in this yeast.


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