Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis
Abstract D-tagatose, a low-calorie rare sugar, has significant potential in food, medicine, cosmetics, and other industries owing to its high application value and market potential. In this study, Escherichia coli BL21 was used as the starting strain to express the β-galactosidase (β-Gal) gene—BgaB—...
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| Format: | Article |
| Language: | English |
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SpringerOpen
2025-02-01
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| Series: | AMB Express |
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| Online Access: | https://doi.org/10.1186/s13568-025-01830-8 |
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| _version_ | 1823861597536256000 |
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| author | Xiaoxiao Zhang Jie Chu Yuanqiang Lv Xuan Li Aijiao Yin Yanhua Huang |
| author_facet | Xiaoxiao Zhang Jie Chu Yuanqiang Lv Xuan Li Aijiao Yin Yanhua Huang |
| author_sort | Xiaoxiao Zhang |
| collection | DOAJ |
| description | Abstract D-tagatose, a low-calorie rare sugar, has significant potential in food, medicine, cosmetics, and other industries owing to its high application value and market potential. In this study, Escherichia coli BL21 was used as the starting strain to express the β-galactosidase (β-Gal) gene—BgaB—derived from Bacillus stearothermophilus and the L-arabinose isomerase (L-AI) gene—araA—derived from Thermus sp., yielding the genetically engineered strains E. coli BL21-pET28a-BgaB and E. coli BL21-pET28a-araA. These strains synthesized D-tagatose using β-Gal and L-AI with a conversion rate of 23.73%. Based on this, we constructed a multienzyme cascade pathway comprising β-Gal, L-AI, glucose isomerase (GI), fructose kinase (FK), D-tagatose-bisphosphate aldolase (GatZ), polyphosphate kinase (PPK), and phosphatase (PGP), further enhancing D-tagatose biosynthesis. This multienzyme approach improved the conversion of the intermediate product D-glucose to D-tagatose by 3.84% compared with the dual-enzyme system. Thus, our study provides a theoretical basis and technical support for the industrial production of D-tagatose. |
| format | Article |
| id | doaj-art-da3ccec83bd04f639e704c1ab95b420d |
| institution | Kabale University |
| issn | 2191-0855 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | AMB Express |
| spelling | doaj-art-da3ccec83bd04f639e704c1ab95b420d2025-02-09T12:55:46ZengSpringerOpenAMB Express2191-08552025-02-0115111010.1186/s13568-025-01830-8Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesisXiaoxiao Zhang0Jie Chu1Yuanqiang Lv2Xuan Li3Aijiao Yin4Yanhua Huang5Biology Institute, Qilu University of Technology (Shandong Academy of Sciences)Biology Institute, Qilu University of Technology (Shandong Academy of Sciences)Biology Institute, Qilu University of Technology (Shandong Academy of Sciences)Biology Institute, Qilu University of Technology (Shandong Academy of Sciences)Biology Institute, Qilu University of Technology (Shandong Academy of Sciences)Biology Institute, Qilu University of Technology (Shandong Academy of Sciences)Abstract D-tagatose, a low-calorie rare sugar, has significant potential in food, medicine, cosmetics, and other industries owing to its high application value and market potential. In this study, Escherichia coli BL21 was used as the starting strain to express the β-galactosidase (β-Gal) gene—BgaB—derived from Bacillus stearothermophilus and the L-arabinose isomerase (L-AI) gene—araA—derived from Thermus sp., yielding the genetically engineered strains E. coli BL21-pET28a-BgaB and E. coli BL21-pET28a-araA. These strains synthesized D-tagatose using β-Gal and L-AI with a conversion rate of 23.73%. Based on this, we constructed a multienzyme cascade pathway comprising β-Gal, L-AI, glucose isomerase (GI), fructose kinase (FK), D-tagatose-bisphosphate aldolase (GatZ), polyphosphate kinase (PPK), and phosphatase (PGP), further enhancing D-tagatose biosynthesis. This multienzyme approach improved the conversion of the intermediate product D-glucose to D-tagatose by 3.84% compared with the dual-enzyme system. Thus, our study provides a theoretical basis and technical support for the industrial production of D-tagatose.https://doi.org/10.1186/s13568-025-01830-8β-GalactosidaseBiosynthesisD-tagatoseL-arabinose isomeraseMultienzyme cascade |
| spellingShingle | Xiaoxiao Zhang Jie Chu Yuanqiang Lv Xuan Li Aijiao Yin Yanhua Huang Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis AMB Express β-Galactosidase Biosynthesis D-tagatose L-arabinose isomerase Multienzyme cascade |
| title | Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis |
| title_full | Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis |
| title_fullStr | Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis |
| title_full_unstemmed | Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis |
| title_short | Construction of a multienzyme cascade reaction system and its application in D-tagatose biosynthesis |
| title_sort | construction of a multienzyme cascade reaction system and its application in d tagatose biosynthesis |
| topic | β-Galactosidase Biosynthesis D-tagatose L-arabinose isomerase Multienzyme cascade |
| url | https://doi.org/10.1186/s13568-025-01830-8 |
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