Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri

Authors
Taranto, MP Sesma, F Font de Valdez, G
Citation
Mp. Taranto et al., Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri, BIOTECH LET, 21(11), 1999, pp. 935-938
Citations number
10
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
BIOTECHNOLOGY LETTERS
ISSN journal
01415492 → ACNP
Volume
21
Issue
11
Year of publication
1999
Pages
935 - 938
Database
ISI
SICI code
0141-5492(199911)21:11<935:LAPCOB>2.0.ZU;2-P
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 degrees C. Th e enzyme (80 kDa apparent mass) has sulphydryl groups in the catalytic acti ve site and hydrolyzes both glycine and taurine conjugated bile acids with higher affinity for glyco-conjugates.