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Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts
- Source :
- Applied and environmental microbiology. 68(6)
- Publication Year :
- 2002
-
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.
- Subjects :
- Taurocholic Acid
Dimer
Stenotrophomonas maltophilia
Kinetics
Glycocholic acid
Applied Microbiology and Biotechnology
digestive system
Amidohydrolases
Bile Acids and Salts
Hydrolysis
chemistry.chemical_compound
Xanthomonas
Animals
Bile
bile salts
Enzymology and Protein Engineering
Ecology
biology
Strain (chemistry)
cholylglycine hydrolase
biology.organism_classification
Taurocholic acid
chemistry
Biochemistry
Cattle
Glycocholic Acid
Food Science
Biotechnology
Subjects
Details
- ISSN :
- 00992240
- Volume :
- 68
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Applied and environmental microbiology
- Accession number :
- edsair.doi.dedup.....f26293502709ccabfe00f7d31a92c2dd