Cholylglycine hydrolase (Bile salt hydrolase) (BSH)

Cholylglycine hydrolase, commonly referred to as bile salt hydrolase (BSH), is a microbial enzyme produced by specific gut bacteria, including the probiotic strain Lactoplantibacillus plantarum CECT7527 (Fuentes et al., 2013; PubMed: 23134431). This enzyme plays a critical role in host lipid metabolism by catalyzing the deconjugation of glycine- or taurine-conjugated bile salts in the gastrointestinal tract (Jones et al., 2008; PubMed: 18403945). Deconjugated bile acids are less soluble and less efficiently reabsorbed through enterohepatic circulation compared to conjugated forms, leading to their increased excretion in feces. To compensate for this loss, the liver upregulates the de novo synthesis of bile acids using systemic cholesterol as a precursor, which results in a significant reduction of circulating total and LDL cholesterol levels (Begley et al., 2006; PubMed: 16396847). Consequently, BSH activity is a primary mechanism by which probiotics like L. plantarum CECT7527 exert cardioprotective and anti-hypercholesterolemic effects. Furthermore, the modification of the bile acid pool by BSH can influence systemic metabolic signaling by altering the availability of ligands for receptors such as the Farnesoid X Receptor (FXR) and TGR5 (Wahlström et al., 2016; PubMed: 26912430).

Other names

Bile salt hydrolaseBSHCholylglycine hydrolaseConjugated bile salt hydrolaseCBAHLactoplantibacillus plantarum CECT7527 BSH

Deconjugation of glycine- and taurine-conjugated bile salts into free bile acids and amino acids, leading to increased fecal excretion and compensatory hepatic cholesterol consumption.