Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i>
Protopanaxadiol-type ginsenosides, the major bioactive components of <i>Panax ginseng</i>, exhibit diverse pharmacological activities, but suffer from low oral bioavailability due to poor water solubility and membrane permeability. Enzymatic deglycosylation has emerged as an effective st...
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2025-05-01
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| author | Jung-Min Choi |
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| description | Protopanaxadiol-type ginsenosides, the major bioactive components of <i>Panax ginseng</i>, exhibit diverse pharmacological activities, but suffer from low oral bioavailability due to poor water solubility and membrane permeability. Enzymatic deglycosylation has emerged as an effective strategy to enhance their therapeutic potential; however, most glucosidases lack sufficient thermostability for industrial applications. A β-glucosidase from the thermophilic bacterium <i>Caldicellulosiruptor bescii</i> (CbBGL) has demonstrated efficient conversion of major ginsenosides into compound K at elevated temperatures. In this study, the high-resolution crystal structure of CbBGL was determined at 1.9 Å. Structural analysis revealed that CbBGL adopts a classical (α/β)<sub>8</sub> TIM barrel fold and functions as a homodimer. Comparative studies with other glucosidases highlighted structural features contributing to its thermostability, including moderate B-factor distribution and a limited hydrogen bond network. Docking analyses revealed a narrow, inverted conical substrate-binding cleft, which imposes specific binding orientations and underlies the enzyme’s stepwise deglycosylation mechanism. These insights provide a structural basis for CbBGL’s thermal resilience and substrate specificity, offering a valuable platform for the rational engineering of glucosidases in ginsenoside bioconversion processes. |
| format | Article |
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| spelling | doaj-art-3741eb81d30d42ab8e8f6671a329861e2025-08-20T02:33:38ZengMDPI AGCrystals2073-43522025-05-0115544710.3390/cryst15050447Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i>Jung-Min Choi0Department of Food Science and Biotechnology, Kyungsung University, Busan 48434, Republic of KoreaProtopanaxadiol-type ginsenosides, the major bioactive components of <i>Panax ginseng</i>, exhibit diverse pharmacological activities, but suffer from low oral bioavailability due to poor water solubility and membrane permeability. Enzymatic deglycosylation has emerged as an effective strategy to enhance their therapeutic potential; however, most glucosidases lack sufficient thermostability for industrial applications. A β-glucosidase from the thermophilic bacterium <i>Caldicellulosiruptor bescii</i> (CbBGL) has demonstrated efficient conversion of major ginsenosides into compound K at elevated temperatures. In this study, the high-resolution crystal structure of CbBGL was determined at 1.9 Å. Structural analysis revealed that CbBGL adopts a classical (α/β)<sub>8</sub> TIM barrel fold and functions as a homodimer. Comparative studies with other glucosidases highlighted structural features contributing to its thermostability, including moderate B-factor distribution and a limited hydrogen bond network. Docking analyses revealed a narrow, inverted conical substrate-binding cleft, which imposes specific binding orientations and underlies the enzyme’s stepwise deglycosylation mechanism. These insights provide a structural basis for CbBGL’s thermal resilience and substrate specificity, offering a valuable platform for the rational engineering of glucosidases in ginsenoside bioconversion processes.https://www.mdpi.com/2073-4352/15/5/447ginsenoside β-glucosidasethermostabilitycrystal structureenzymatic deglycosylation |
| spellingShingle | Jung-Min Choi Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i> Crystals ginsenoside β-glucosidase thermostability crystal structure enzymatic deglycosylation |
| title | Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i> |
| title_full | Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i> |
| title_fullStr | Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i> |
| title_full_unstemmed | Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i> |
| title_short | Structural Study of Thermostable Ginsenoside β-Glucosidase from <i>Caldicellulosiruptor bescii</i> |
| title_sort | structural study of thermostable ginsenoside β glucosidase from i caldicellulosiruptor bescii i |
| topic | ginsenoside β-glucosidase thermostability crystal structure enzymatic deglycosylation |
| url | https://www.mdpi.com/2073-4352/15/5/447 |
| work_keys_str_mv | AT jungminchoi structuralstudyofthermostableginsenosidebglucosidasefromicaldicellulosiruptorbesciii |