New insight into the catalytic properties of bile salt hydrolase |
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| Institution: | 1. Key Laboratory of Education Ministry, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu 214122, China;2. School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu 214122, China;3. Shandong Peanut Research Institute, 126 Fushan Road, Qingdao, Shandong 266100, China;1. Innovation Division, KAGOME Co., Ltd., 17 Nishitomiyama, Nasushiobara, Tochigi 329-2762, Japan;2. Laboratory of Microbial Technology, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka-shi, Fukuoka 819-0395, Japan;1. Department of Pharmacology and Toxicology, Faculty of Pharmacy, Charles University in Prague, Heyrovského 1203, Hradec Kralove CZ500 05, Czechia;2. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ160 00 Praha, Czechia;3. Regional Centre of Advanced Technologies and Materials, Department of Physical Chemistry, Palacky University in Olomouc, 17. listopadu 1131, Olomouc CZ779 00, Czechia;4. Department of Internal Medicine IV, Gastroenterology and Infectious Diseases, Im Neuenheimer Feld, Heidelberg, Germany;1. University of North Carolina-Chapel Hill Department of Psychiatry, United States;2. Uppsala University, Department of Women and Children’s Health, Sweden;3. University of North Carolina-Chapel Hill Gillings School of Public Health, United States;4. University of North Carolina-Chapel Hill Department of Medicine and UNC Microbiome Core, United States;5. University of North Carolina-Chapel Hill School of Public Health Department of Nutrition, United States;6. Department of Microbiology, Tumor and Cell Biology, Karolinska Insitutet Centre for Translational Microbiome Research, Sweden;7. Michigan State University Department of Pediatrics and Human Development, United States;8. Williams College Department of Mathematics and Statistics, United States;1. Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland;2. Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing, People''s Republic of China;3. Department of Veterinary and Biomedical Sciences and the Center for Molecular Toxicology and Carcinogenesis, The Pennsylvania State University, University Park, Pennsylvania;1. Department of Gastroenterology, Ghent University Hospital, Ghent, Belgium |
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| Abstract: | Bile salt hydrolase (BSH), the enzyme deconjugating bile potentially plays an important role in reduction of blood cholesterol level. BSH enzymes from various sources differ in characteristics, substrates preference and specific catalytic activity. In this study, two BSH enzymes (BSH1 and BSH2) from Lactobacillus salivarius were heterologously expressed and purified. Both of them were characterized as homotetramer according to their molecular weight from size exclusion chromatograph. BSH1 showed a broad pH optimum over the range from 5.5 to 7.0, while a narrower range of pH optimum from 5.5 to 6.0 for BSH2 was detected. The enzymatic kinetics of the purified BSH1 and BSH2 have demonstrated BSH enzymes from bacteria were allosteric enzymes, and have also revealed their striking differences in positive cooperativity, catalytic efficiency and substrate preference for the first time. In contrast to the enzymatic reactions of BSH in the absence of dithiothreitol, the kinetics curves of BSH1 and BSH2 were similar to hyperbolic forms of Michaelis–Menten kinetics in the presence of dithiothreitol. |
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| Keywords: | Bile salt hydrolase Bile Cholesterol Allosteric regulation |
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