Expression of bacterial β-glucuronidase in human bile: An in vitro study

Joseph Leung, Yan Lei Liu, Patrick S Leung, Raphael C Y Chan, John F. Inciardi, Augustine F. Cheng

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Background: Bacterial β-glucuronidase causes deconjugation of bilirubin diglucuronide resulting in the precipitation of calcium bilirubinate, which contributes to biliary sludge and stone formation. This process is attributed to enzyme activity produced by the aerobic enterobacteriaceae such as Escherichia coli and Klebsiella sp. The presence of Clostridium sp. was detected in 48 of 56 intrahepatic stones by using polymerase chain reaction techniques and cultured Clostridium perfringens from 14 of 18 unblocked biliary stents. Such bacteria are reported to produce β-glucuronidase activity. The aim of this study was to determine the proportion of biliary bacteria isolated from pigment stones and stents that produce β-glucuronidase and to compare the enzyme activity expressed by the different bacteria in human bile. Methods: A total of 202 bacteria were isolated from blocked and unblocked biliary stents and pigment ductal stones recovered from patients. Of these, 61 bacteria expressed β-glucuronidase activity in brain heart infusion broth. These 61 bacteria were subsequently grown in human bile under aerobic or anaerobic conditions to the early stationary phase and assayed for β-glucuronidase activity by using p-nitrophenyl β-D glucuronide as substrate. Results were normalized and reported as units of enzyme activity per milligram protein of the bacteria. Results: C perfringens produced β-glucuronidase enzyme activity that was 34-fold higher than that for E coli, Staphylococcus, Corynebacterium sp., Bacillus sp., Enterococcus sp., Acinetobacter sp., Streptococcus sp., and Klebsiella sp. Conclusion: C perfringens with its higher enzyme activity is more important in the deconjugation of bilirubin diglucuronide than E coli and Klebsiella sp.

Original languageEnglish (US)
Pages (from-to)346-350
Number of pages5
JournalGastrointestinal Endoscopy
Volume54
Issue number3
DOIs
StatePublished - Sep 2001

Fingerprint

Glucuronidase
Bile
Bacteria
Klebsiella
Stents
Enzymes
Escherichia coli
Corynebacterium
Clostridium perfringens
Acinetobacter
Clostridium
Glucuronides
Enterococcus
Enterobacteriaceae
In Vitro Techniques
Streptococcus
Staphylococcus
Bilirubin
Bacillus
Polymerase Chain Reaction

ASJC Scopus subject areas

  • Gastroenterology

Cite this

Expression of bacterial β-glucuronidase in human bile : An in vitro study. / Leung, Joseph; Liu, Yan Lei; Leung, Patrick S; Chan, Raphael C Y; Inciardi, John F.; Cheng, Augustine F.

In: Gastrointestinal Endoscopy, Vol. 54, No. 3, 09.2001, p. 346-350.

Research output: Contribution to journalArticle

Leung, Joseph ; Liu, Yan Lei ; Leung, Patrick S ; Chan, Raphael C Y ; Inciardi, John F. ; Cheng, Augustine F. / Expression of bacterial β-glucuronidase in human bile : An in vitro study. In: Gastrointestinal Endoscopy. 2001 ; Vol. 54, No. 3. pp. 346-350.
@article{d58a4e8afe7640fa8c6a3db98d2afcc9,
title = "Expression of bacterial β-glucuronidase in human bile: An in vitro study",
abstract = "Background: Bacterial β-glucuronidase causes deconjugation of bilirubin diglucuronide resulting in the precipitation of calcium bilirubinate, which contributes to biliary sludge and stone formation. This process is attributed to enzyme activity produced by the aerobic enterobacteriaceae such as Escherichia coli and Klebsiella sp. The presence of Clostridium sp. was detected in 48 of 56 intrahepatic stones by using polymerase chain reaction techniques and cultured Clostridium perfringens from 14 of 18 unblocked biliary stents. Such bacteria are reported to produce β-glucuronidase activity. The aim of this study was to determine the proportion of biliary bacteria isolated from pigment stones and stents that produce β-glucuronidase and to compare the enzyme activity expressed by the different bacteria in human bile. Methods: A total of 202 bacteria were isolated from blocked and unblocked biliary stents and pigment ductal stones recovered from patients. Of these, 61 bacteria expressed β-glucuronidase activity in brain heart infusion broth. These 61 bacteria were subsequently grown in human bile under aerobic or anaerobic conditions to the early stationary phase and assayed for β-glucuronidase activity by using p-nitrophenyl β-D glucuronide as substrate. Results were normalized and reported as units of enzyme activity per milligram protein of the bacteria. Results: C perfringens produced β-glucuronidase enzyme activity that was 34-fold higher than that for E coli, Staphylococcus, Corynebacterium sp., Bacillus sp., Enterococcus sp., Acinetobacter sp., Streptococcus sp., and Klebsiella sp. Conclusion: C perfringens with its higher enzyme activity is more important in the deconjugation of bilirubin diglucuronide than E coli and Klebsiella sp.",
author = "Joseph Leung and Liu, {Yan Lei} and Leung, {Patrick S} and Chan, {Raphael C Y} and Inciardi, {John F.} and Cheng, {Augustine F.}",
year = "2001",
month = "9",
doi = "10.1067/mge.2001.117546",
language = "English (US)",
volume = "54",
pages = "346--350",
journal = "Gastrointestinal Endoscopy",
issn = "0016-5107",
publisher = "Mosby Inc.",
number = "3",

}

TY - JOUR

T1 - Expression of bacterial β-glucuronidase in human bile

T2 - An in vitro study

AU - Leung, Joseph

AU - Liu, Yan Lei

AU - Leung, Patrick S

AU - Chan, Raphael C Y

AU - Inciardi, John F.

AU - Cheng, Augustine F.

PY - 2001/9

Y1 - 2001/9

N2 - Background: Bacterial β-glucuronidase causes deconjugation of bilirubin diglucuronide resulting in the precipitation of calcium bilirubinate, which contributes to biliary sludge and stone formation. This process is attributed to enzyme activity produced by the aerobic enterobacteriaceae such as Escherichia coli and Klebsiella sp. The presence of Clostridium sp. was detected in 48 of 56 intrahepatic stones by using polymerase chain reaction techniques and cultured Clostridium perfringens from 14 of 18 unblocked biliary stents. Such bacteria are reported to produce β-glucuronidase activity. The aim of this study was to determine the proportion of biliary bacteria isolated from pigment stones and stents that produce β-glucuronidase and to compare the enzyme activity expressed by the different bacteria in human bile. Methods: A total of 202 bacteria were isolated from blocked and unblocked biliary stents and pigment ductal stones recovered from patients. Of these, 61 bacteria expressed β-glucuronidase activity in brain heart infusion broth. These 61 bacteria were subsequently grown in human bile under aerobic or anaerobic conditions to the early stationary phase and assayed for β-glucuronidase activity by using p-nitrophenyl β-D glucuronide as substrate. Results were normalized and reported as units of enzyme activity per milligram protein of the bacteria. Results: C perfringens produced β-glucuronidase enzyme activity that was 34-fold higher than that for E coli, Staphylococcus, Corynebacterium sp., Bacillus sp., Enterococcus sp., Acinetobacter sp., Streptococcus sp., and Klebsiella sp. Conclusion: C perfringens with its higher enzyme activity is more important in the deconjugation of bilirubin diglucuronide than E coli and Klebsiella sp.

AB - Background: Bacterial β-glucuronidase causes deconjugation of bilirubin diglucuronide resulting in the precipitation of calcium bilirubinate, which contributes to biliary sludge and stone formation. This process is attributed to enzyme activity produced by the aerobic enterobacteriaceae such as Escherichia coli and Klebsiella sp. The presence of Clostridium sp. was detected in 48 of 56 intrahepatic stones by using polymerase chain reaction techniques and cultured Clostridium perfringens from 14 of 18 unblocked biliary stents. Such bacteria are reported to produce β-glucuronidase activity. The aim of this study was to determine the proportion of biliary bacteria isolated from pigment stones and stents that produce β-glucuronidase and to compare the enzyme activity expressed by the different bacteria in human bile. Methods: A total of 202 bacteria were isolated from blocked and unblocked biliary stents and pigment ductal stones recovered from patients. Of these, 61 bacteria expressed β-glucuronidase activity in brain heart infusion broth. These 61 bacteria were subsequently grown in human bile under aerobic or anaerobic conditions to the early stationary phase and assayed for β-glucuronidase activity by using p-nitrophenyl β-D glucuronide as substrate. Results were normalized and reported as units of enzyme activity per milligram protein of the bacteria. Results: C perfringens produced β-glucuronidase enzyme activity that was 34-fold higher than that for E coli, Staphylococcus, Corynebacterium sp., Bacillus sp., Enterococcus sp., Acinetobacter sp., Streptococcus sp., and Klebsiella sp. Conclusion: C perfringens with its higher enzyme activity is more important in the deconjugation of bilirubin diglucuronide than E coli and Klebsiella sp.

UR - http://www.scopus.com/inward/record.url?scp=0035463856&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035463856&partnerID=8YFLogxK

U2 - 10.1067/mge.2001.117546

DO - 10.1067/mge.2001.117546

M3 - Article

C2 - 11522976

AN - SCOPUS:0035463856

VL - 54

SP - 346

EP - 350

JO - Gastrointestinal Endoscopy

JF - Gastrointestinal Endoscopy

SN - 0016-5107

IS - 3

ER -