Danyun Wang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Danyun Wang has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Hongyu Zhang
Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin, China
2 shared publications - Suying Wang
Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China
2 shared publications - Tingting Lou
Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China
2 shared publications - Zixuan Zhou
Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China
2 shared publications - Deguang Zhang
Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China
1 shared publication - Jinshan Yang
Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China
1 shared publication
Latest Publications
- Open Access
Advancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products
Sucrose phosphorylase (SPase), a member of the glycoside hydrolase GH13 family, possesses the ability to catalyze the hydrolysis of sucrose to generate α-glucose-1-phosphate and can also glycosylate diverse substrates, showcasing a wide substrate specificity. This enzyme has found extensive utility in the fields of food, medicine, and cosmetics, and has garnered significant attention as a focal point of research in transglycosylation enzymes. Nevertheless, SPase encounters numerous obstacles in industrial settings, including low enzyme yield, inadequate thermal stability, mixed regioselectivity, and limited transglycosylation activity. In-depth exploration of efficient expression strategies and molecular modifications based on the crystal structure and functional information of SPase is now a critical research priority. This paper systematically reviews the source microorganisms, crystal structure, and catalytic mechanism of SPase, summarizes diverse heterologous expression systems based on expression hosts and vectors, and examines the application and molecular modification progress of SPase in synthesizing typical glycosylated products. Additionally, it anticipates the broad application prospects of SPase in industrial production and related research fields, laying the groundwork for its engineering modification and industrial application.
Open AccessAdvancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products
Sucrose phosphorylase (SPase), a member of the glycoside hydrolase GH13 family, possesses the ability to catalyze the hydrolysis of sucrose to generate α-glucose-1-phosphate and can also glycosylate diverse substrates, showcasing a wide substrate specificity. This enzyme has found extensive utility in the fields of food, medicine, and cosmetics, and has garnered significant attention as a focal point of research in transglycosylation enzymes. Nevertheless, SPase encounters numerous obstacles in industrial settings, including low enzyme yield, inadequate thermal stability, mixed regioselectivity, and limited transglycosylation activity. In-depth exploration of efficient expression strategies and molecular modifications based on the crystal structure and functional information of SPase is now a critical research priority. This paper systematically reviews the source microorganisms, crystal structure, and catalytic mechanism of SPase, summarizes diverse heterologous expression systems based on expression hosts and vectors, and examines the application and molecular modification progress of SPase in synthesizing typical glycosylated products. Additionally, it anticipates the broad application prospects of SPase in industrial production and related research fields, laying the groundwork for its engineering modification and industrial application.
- Open Access
- 28 August 2023
- Published by MDPI AG in Fermentation
- Vol. 9 (9) , 795
Advance in Heterologous Expression of Biomass-Degrading Auxiliary Activity 10 Family of Lytic Polysaccharide Monooxygenases
AA10 family lytic polysaccharide monooxygenases (AA10 LPMOs) are mainly distributed in bacteria. Because of their characteristics of oxidative degradation of crystalline polysaccharides, such as cellulose and chitin, they have great application potential in industrial biomass conversion and have attracted wide attention. Efficient heterologous expression of LPMOs by recombinant engineering bacteria has become the main strategy for the industrial production of enzymes. The research progress of AA10 LPMOs’ heterologous expression systems was reviewed in this paper. The construction strategies of its diversified heterologous expression system were introduced based on the design and processing of the expression host, vector, and LPMOs gene. The effects of different expression systems on the soluble expression of LPMOs and the development direction of the construction of LPMOs’ heterologous expression systems were discussed. The broad application prospect of LPMOs in the biomass conversion and biofuel industry has been prospected.
- 28 August 2023
- Published by MDPI AG in Fermentation
- Vol. 9 (9) , 795
Open AccessAdvance in Heterologous Expression of Biomass-Degrading Auxiliary Activity 10 Family of Lytic Polysaccharide Monooxygenases
AA10 family lytic polysaccharide monooxygenases (AA10 LPMOs) are mainly distributed in bacteria. Because of their characteristics of oxidative degradation of crystalline polysaccharides, such as cellulose and chitin, they have great application potential in industrial biomass conversion and have attracted wide attention. Efficient heterologous expression of LPMOs by recombinant engineering bacteria has become the main strategy for the industrial production of enzymes. The research progress of AA10 LPMOs’ heterologous expression systems was reviewed in this paper. The construction strategies of its diversified heterologous expression system were introduced based on the design and processing of the expression host, vector, and LPMOs gene. The effects of different expression systems on the soluble expression of LPMOs and the development direction of the construction of LPMOs’ heterologous expression systems were discussed. The broad application prospect of LPMOs in the biomass conversion and biofuel industry has been prospected.