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Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing beta-glucuronidase from Staphylococcus pasteuri 3I10
Wei, Bin1; Wang, Pan-Pan1; Yan, Zhi-Xiang1; Yan, Ru1,2
2018-11
Source PublicationAPPLIED MICROBIOLOGY AND BIOTECHNOLOGY
ISSN0175-7598
Volume102Issue:21Pages:9193-9205
AbstractGlycyrrhizin (GL), the principal sweet-tasting bioactive ingredient of licorice (root of Glycyrrhiza glabra), shows poor oral absorption and gut microbial transformation of GL to glycyrrhetinic acid (GA) plays a major role for its multiple pharmacological effects. Co-administration of GL-hydrolyzing bacteria appears to be a feasible strategy to enhance GA exposure. This study reported a gut bacterial strain Staphylococcus pasteuri 3I10 which exhibited moderate p-nitrophenyl-beta-D-glucuronide (PNPG)-hydrolyzing activity but low GL deglucuronidation activity in its crude lysate. The gus gene encoding S. pasteuri 3I10 beta-glucuronidase was successfully cloned and overexpressed in Escherichia coli BL21(DE3). The purified beta-glucuronidase (SpasGUS) was 71 kDa and showed optimal pH and temperature at 6.0 and 50 degrees C, respectively. Comparing to E. coli beta-glucuronidase (EcoGUS), SpasGUS displayed lower velocity and affinity to PNPG hydrolysis (V-max 16.1 +/- 0.9 vs 140.0 +/- 4.1 mu molmin(-1) mg(-1); K-m 469.4 +/- 73.4 vs 268.0 +/- 25.8 mu M), but could selectively convert GL to GA at much higher efficiency (V-max 0.41 +/- 0.011 vs 0.005 +/- 0.002 mu molmin(-1) mg(-1); K-m 116.9 +/- 15.4 vs 53.4 +/- 34.8 mu M). Molecular docking studies suggested SpasGUS formed hydrogen bond interactions with the glucuronic acids at Asn414, Glu415 and Leu450, and Val159, Tyr475, Ala368, and Phe367 provided a hydrophobic environment for enhanced activity. Two special substrate interaction loops near the binding pocket of SpasGUS (loop 1 beta-glucuronidase) may account for the selective and efficient bioconversion of GL to GA, predicting that loop 1 beta-glucuronidases show high possibility in processing GL than mini-loop 1 and loop 2 beta-glucuronidases. These findings support potential applications of SpasGUS in cleaving GL to facilitate GA production in vivo or in pharmaceutical industry.
KeywordStaphylococcus pasteuri Bacterial beta-glucuronidase Glycyrrhizin Glycyrrhetinic acid Deglucuronidation Homology modeling
DOI10.1007/s00253-018-9285-x
URLView the original
Indexed BySCI
Language英语
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000448359000015
PublisherSPRINGER
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Cited Times [WOS]:1   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionUniversity of Macau
Affiliation1.Univ Macau, Inst Chinese Med Sci, State Key Lab Qual Res Chinese Med, Taipa, Macao, Peoples R China;
2.Zhuhai UM Sci & Technol Res Inst, Zhuhai 519080, Peoples R China
First Author AffilicationUniversity of Macau
Recommended Citation
GB/T 7714
Wei, Bin,Wang, Pan-Pan,Yan, Zhi-Xiang,et al. Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing beta-glucuronidase from Staphylococcus pasteuri 3I10[J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,2018,102(21):9193-9205.
APA Wei, Bin,Wang, Pan-Pan,Yan, Zhi-Xiang,&Yan, Ru.(2018).Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing beta-glucuronidase from Staphylococcus pasteuri 3I10.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,102(21),9193-9205.
MLA Wei, Bin,et al."Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing beta-glucuronidase from Staphylococcus pasteuri 3I10".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 102.21(2018):9193-9205.
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