Bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids). Can hydrolyze the amid bond in all six major human bile salts, namely glycocholate (GCA), glycodeoxycholate (GDCA), glycochenodeoxycholate (GCDCA), taurocholate (TCA), taurodeoxycholate (TDCA) and taurochenodeoxycholate (TCDCA). Shows a slight preference for glycine-conjugated bile acids as substrates (PubMed:10831430, PubMed:16905539). Is totally inactive toward penicillin V (PubMed:16905539). glycocholate + H2O = cholate + glycine glycodeoxycholate + H2O = deoxycholate + glycine chenodeoxycholate + glycine = glycochenodeoxycholate + H2O cholate + taurine = H2O + taurocholate H2O + taurodeoxycholate = deoxycholate + taurine H2O + taurochenodeoxycholate = chenodeoxycholate + taurine Competitively inhibited by the products cholate (CA) and deoxycholate (DCA), and by phenylacetate and 4-aminophenylacetate. Penicillin V and penicillin G show mixed inhibition (PubMed:16905539). Strongly inhibited by thiol enzyme inhibitors in vitro (PubMed:10831430). kcat is 85 sec(-1) with glycocholate as substrate. kcat is 76 sec(-1) with taurocholate as substrate (at 40 degrees Celsius and pH 6.5). Optimum pH is 6. Highly active in the pH range 5-7. Is stable at pH values from 4 to 8. At pH values above 8 and below 4 the enzyme is rapidly inactivated. Optimum temperature is 40-45 degrees Celsius. Is stable at temperatures from 4 to 37 degrees Celsius. During 30 minutes of incubation at 40 degrees Celsius, about 20 to 30% of the activity is lost, and at 50 degrees Celsius only 20% of the activity is retained. Lipid metabolism; bile acid biosynthesis. Homotetramer (PubMed:10831430, PubMed:16905539). The tetramer consists of a dimer of dimers (PubMed:16905539). Is part of an operon containing at least two genes, bsh and glnE (GlnE is glutamine synthetase adenylyltransferase). Belongs to the peptidase C59 family.