Bile salt hydrolase (BSH) is an intracellular enzyme produced by certain bacterial species in the intestinal microbiota.It plays a crucial role in bile salt hydrolysis.This study aimed to investigate BSH enzymatic properties and structural characteristics by expressing of BSH from Lactiplantibacillus plantarum (LpBSH) in E.coli.Recombinant BSH expression system was constructed, and its enzymatic properties were examined.The three-dimensiona structure, active site, and substrate-binding pocket of LpBSH were predicted and analyzed by bioinformatics methods.The results showed that the activity of the recombinant LpBSH was 88.7 U/mL, significantly higher than the wild-type.The recombinant LpBSH had the highest activity at pH 6.5.K+ slightly increased the hydrolysis activity of LpBSH, while heavy metal ions generally inhibited the activity.Kinetic studies revealed that BSH catalysis follows the Hill equation, indicating homotropic interaction.The analysis of the predicted structural model and expremental data revealed key relationships between sequence, active site, substrate-binding pocket, and substrate preference.This study laid the foundation for further understanding the structure-function relationship of BSH and its role in animal cholesterol metabolism, and provided a scientific basis for the development of BSH enzyme preparations.
YAN Zhihao
,
SHI Jian
,
ZHU Yuhong
,
ZHOU Jin
,
WANG Guokang
,
GAN Ling
,
GUO Jianhua
. Prokaryotic expression, enzymatic characteristics, and bioinformatic analysis of bile salt hydrolase from Lactiplantibacillus plantarum[J]. Food and Fermentation Industries, 2025
, 51(13)
: 29
-37
.
DOI: 10.13995/j.cnki.11-1802/ts.040721
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