Bibliographic Details
| Title: |
Advancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products |
| Authors: |
Hongyu Zhang, Leting Zhu, Zixuan Zhou, Danyun Wang, Jinshan Yang, Suying Wang, Tingting Lou |
| Source: |
Molecules, Vol 29, Iss 17, p 4086 (2024) |
| Publisher Information: |
MDPI AG, 2024. |
| Publication Year: |
2024 |
| Collection: |
LCC:Organic chemistry |
| Subject Terms: |
sucrose phosphorylase, transglycosylation, catalytic mechanism, heterologous expression, molecular modification, Organic chemistry, QD241-441 |
| More Details: |
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. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
1420-3049 |
| Relation: |
https://www.mdpi.com/1420-3049/29/17/4086; https://doaj.org/toc/1420-3049 |
| DOI: |
10.3390/molecules29174086 |
| Access URL: |
https://doaj.org/article/951ac7a8a01f4bbc90cd76b0497c2f5e |
| Accession Number: |
edsdoj.951ac7a8a01f4bbc90cd76b0497c2f5e |
| Database: |
Directory of Open Access Journals |
|
Full text is not displayed to guests. |
Login for full access.
|
