Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta
D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructos...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2020-12-01
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| Series: | Frontiers in Chemistry |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fchem.2020.622325/full |
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| author | Yang Wang Yuvaraj Ravikumar Guoyan Zhang Junhua Yun Yufei Zhang Amreesh Parvez Xianghui Qi Xianghui Qi Wenjing Sun |
| author_facet | Yang Wang Yuvaraj Ravikumar Guoyan Zhang Junhua Yun Yufei Zhang Amreesh Parvez Xianghui Qi Xianghui Qi Wenjing Sun |
| author_sort | Yang Wang |
| collection | DOAJ |
| description | D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEase that works at acidic conditions is highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on -fructose at pH 6.0 and 50°C with a Kcat/Km value of 45 mM−1min−1. The 500 g/L D-fructose, which corresponded to 30% conversion rate. With these interesting catalytic properties, this enzyme could be a promising candidate for industrial biocatalytic applications. |
| first_indexed | 2024-12-14T16:56:36Z |
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| institution | Directory Open Access Journal |
| issn | 2296-2646 |
| language | English |
| last_indexed | 2024-12-14T16:56:36Z |
| publishDate | 2020-12-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Chemistry |
| spelling | doaj.art-d81bafd2824f4caeaa383886ffe7a2462022-12-21T22:53:57ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462020-12-01810.3389/fchem.2020.622325622325Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minutaYang Wang0Yuvaraj Ravikumar1Guoyan Zhang2Junhua Yun3Yufei Zhang4Amreesh Parvez5Xianghui Qi6Xianghui Qi7Wenjing Sun8School of Life Science, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaSchool of Life Science, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, ChinaD-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEase that works at acidic conditions is highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on -fructose at pH 6.0 and 50°C with a Kcat/Km value of 45 mM−1min−1. The 500 g/L D-fructose, which corresponded to 30% conversion rate. With these interesting catalytic properties, this enzyme could be a promising candidate for industrial biocatalytic applications.https://www.frontiersin.org/articles/10.3389/fchem.2020.622325/fullD-tagatose 3-epimeraseD-alluloseChristensenella minutabiochemical characterizationbiocatalysis |
| spellingShingle | Yang Wang Yuvaraj Ravikumar Guoyan Zhang Junhua Yun Yufei Zhang Amreesh Parvez Xianghui Qi Xianghui Qi Wenjing Sun Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta Frontiers in Chemistry D-tagatose 3-epimerase D-allulose Christensenella minuta biochemical characterization biocatalysis |
| title | Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta |
| title_full | Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta |
| title_fullStr | Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta |
| title_full_unstemmed | Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta |
| title_short | Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta |
| title_sort | biocatalytic synthesis of d allulose using novel d tagatose 3 epimerase from christensenella minuta |
| topic | D-tagatose 3-epimerase D-allulose Christensenella minuta biochemical characterization biocatalysis |
| url | https://www.frontiersin.org/articles/10.3389/fchem.2020.622325/full |
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