Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides
The GH43 family of glycosidases represents an important class of industrial enzymes that are widely utilized across the food, pharmaceutical, and various other sectors. In this study, we identified a GH43 family glycoside hydrolytic enzyme, <i>Xyaf313</i>, derived from the plant endophyt...
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2025-03-01
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| author | Yao Lu Qiang Jiang Yamin Dong Runzhen Ji Yiwen Xiao Du Zhu Boliang Gao |
| author_facet | Yao Lu Qiang Jiang Yamin Dong Runzhen Ji Yiwen Xiao Du Zhu Boliang Gao |
| author_sort | Yao Lu |
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| description | The GH43 family of glycosidases represents an important class of industrial enzymes that are widely utilized across the food, pharmaceutical, and various other sectors. In this study, we identified a GH43 family glycoside hydrolytic enzyme, <i>Xyaf313</i>, derived from the plant endophytic fungus <i>Chaetomium globosum</i> DX-THS3, which is capable of transforming several common ginsenosides. The enzyme function analysis reveals that Xyaf313 exhibits dual functionality, displaying both α-L-arabinofuranosidase and β-D-xylosidase activity. When acting as an α-L-arabinofuranosidase, Xyaf313 achieves optimal enzyme activity of 23.96 U/mg at a temperature of 50 °C and a pH of 7. In contrast, its β-D-xylosidase activity results in a slight reduction in enzyme activity to 23.24 U/mg, with similar optimal temperature and pH conditions to those observed for the α-L-arabinofuranosidase activity. Furthermore, Xyaf313 demonstrates considerable resistance to most metal ions and common chemical reagents. Notably, while the maximum enzyme activity of Xyaf313 occurs at 50 °C, it maintains high activity at room temperature (30 °C), with relative enzyme activity exceeding 90%. Measurements of ginsenoside transformation show that Xyaf313 can convert common ginsenosides Rc, Rb<sub>1</sub>, Rb<sub>2</sub>, and Rb<sub>3</sub> into Rd, underscoring its potential for pharmaceutical applications. Overall, our findings contribute to the identification of a new class of bifunctional GH43 glycoside hydrolases, highlight the significance of plant endophytic fungi as a promising resource for the screening of carbohydrate-decomposing enzymes, and present new candidate enzymes for the biotransformation of ginsenosides. |
| format | Article |
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| spelling | doaj-art-e5bb730617664c64a4b12ef3ec0f544e2025-08-20T02:11:09ZengMDPI AGBioTech2673-62842025-03-011411810.3390/biotech14010018Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of GinsenosidesYao Lu0Qiang Jiang1Yamin Dong2Runzhen Ji3Yiwen Xiao4Du Zhu5Boliang Gao6Key Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaKey Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaKey Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaKey Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaKey Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaKey Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaKey Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, ChinaThe GH43 family of glycosidases represents an important class of industrial enzymes that are widely utilized across the food, pharmaceutical, and various other sectors. In this study, we identified a GH43 family glycoside hydrolytic enzyme, <i>Xyaf313</i>, derived from the plant endophytic fungus <i>Chaetomium globosum</i> DX-THS3, which is capable of transforming several common ginsenosides. The enzyme function analysis reveals that Xyaf313 exhibits dual functionality, displaying both α-L-arabinofuranosidase and β-D-xylosidase activity. When acting as an α-L-arabinofuranosidase, Xyaf313 achieves optimal enzyme activity of 23.96 U/mg at a temperature of 50 °C and a pH of 7. In contrast, its β-D-xylosidase activity results in a slight reduction in enzyme activity to 23.24 U/mg, with similar optimal temperature and pH conditions to those observed for the α-L-arabinofuranosidase activity. Furthermore, Xyaf313 demonstrates considerable resistance to most metal ions and common chemical reagents. Notably, while the maximum enzyme activity of Xyaf313 occurs at 50 °C, it maintains high activity at room temperature (30 °C), with relative enzyme activity exceeding 90%. Measurements of ginsenoside transformation show that Xyaf313 can convert common ginsenosides Rc, Rb<sub>1</sub>, Rb<sub>2</sub>, and Rb<sub>3</sub> into Rd, underscoring its potential for pharmaceutical applications. Overall, our findings contribute to the identification of a new class of bifunctional GH43 glycoside hydrolases, highlight the significance of plant endophytic fungi as a promising resource for the screening of carbohydrate-decomposing enzymes, and present new candidate enzymes for the biotransformation of ginsenosides.https://www.mdpi.com/2673-6284/14/1/18α-L-arabinofuranosidaseβ-D-xylosidasebiotransformationendophytic fungiGH43 family |
| spellingShingle | Yao Lu Qiang Jiang Yamin Dong Runzhen Ji Yiwen Xiao Du Zhu Boliang Gao Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides BioTech α-L-arabinofuranosidase β-D-xylosidase biotransformation endophytic fungi GH43 family |
| title | Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides |
| title_full | Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides |
| title_fullStr | Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides |
| title_full_unstemmed | Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides |
| title_short | Characterization of a GH43 Bifunctional Glycosidase from Endophytic <i>Chaetomium globosum</i> and Its Potential Application in the Biotransformation of Ginsenosides |
| title_sort | characterization of a gh43 bifunctional glycosidase from endophytic i chaetomium globosum i and its potential application in the biotransformation of ginsenosides |
| topic | α-L-arabinofuranosidase β-D-xylosidase biotransformation endophytic fungi GH43 family |
| url | https://www.mdpi.com/2673-6284/14/1/18 |
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