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Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing β-glucuronidase from Staphylococcus pasteuri 3I10
Bin Wei1; Pan-Pan Wang1; Zhi-Xiang Yan1; Ru Yan1,2
2018-08-14
Source PublicationApplied Microbiology and Biotechnology
ISSN0175-7598
Volume102Issue:21Pages:9193–9205
Abstract

Glycyrrhizin (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-β-D-glucuronide (PNPG)-hydrolyzing activity but low GL deglucuronidation activity in its crude lysate. The gus gene encoding S. pasteuri 3I10 β-glucuronidase was successfully cloned and overexpressed in Escherichia coli BL21(DE3). The purified β-glucuronidase (SpasGUS) was 71 kDa and showed optimal pH and temperature at 6.0 and 50 °C, respectively. Comparing to E. coli β-glucuronidase (EcoGUS), SpasGUS displayed lower velocity and affinity to PNPG hydrolysis (Vmax 16.1 ± 0.9 vs 140.0 ± 4.1 μmolmin−1 mg−1; Km 469.4 ± 73.4 vs 268.0 ± 25.8 μM), but could selectively convert GL to GA at much higher efficiency (Vmax 0.41 ± 0.011 vs 0.005 ± 0.002 μmolmin−1 mg−1; Km 116.9 ± 15.4 vs 53.4 ± 34.8 μM). 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 β-glucuronidase) may account for the selective and efficient bioconversion of GL to GA, predicting that loop 1 β-glucuronidases show high possibility in processing GL than mini-loop 1 and loop 2 β-glucuronidases. These findings support potential applications of SpasGUS in cleaving GL to facilitate GA production in vivo or in pharmaceutical industry.

KeywordStaphylococcus Pasteuri Bacterial Β-glucuronidase Glycyrrhizin Glycyrrhetinic Acid Deglucuronidation Homologymodeling
DOIhttps://doi.org/10.1007/s00253-018-9285-x
Indexed BySCI
Language英语
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000448359000015
PublisherSPRINGER, 233 SPRING ST, NEW YORK, NY 10013 USA
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Cited Times [WOS]:3   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionInstitute of Chinese Medical Sciences
Corresponding AuthorRu Yan
Affiliation1.State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Taipa, Macao, China
2.Zhuhai UM Science & Technology Research Institute, Zhuhai 519080, China
First Author AffilicationInstitute of Chinese Medical Sciences
Corresponding Author AffilicationInstitute of Chinese Medical Sciences
Recommended Citation
GB/T 7714
Bin Wei,Pan-Pan Wang,Zhi-Xiang Yan,et al. Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing β-glucuronidase from Staphylococcus pasteuri 3I10[J]. Applied Microbiology and Biotechnology,2018,102(21):9193–9205.
APA Bin Wei,Pan-Pan Wang,Zhi-Xiang Yan,&Ru Yan.(2018).Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing β-glucuronidase from Staphylococcus pasteuri 3I10.Applied Microbiology and Biotechnology,102(21),9193–9205.
MLA Bin Wei,et al."Characteristics and molecular determinants of a highly selective and efficient glycyrrhizin-hydrolyzing β-glucuronidase from Staphylococcus pasteuri 3I10".Applied Microbiology and Biotechnology 102.21(2018):9193–9205.
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