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Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides

Food Science and Technology

Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides

J. Zhang, M. Tang, et al.

Dive into the world of sweeteners as researchers Jinzhu Zhang and colleagues reveal the secrets of OsUGT91C1, a rice glycosyltransferase that enhances the production of Steviol glycosides, the natural sweeteners from *Stevia rebaudiana*. Their innovative approach promises not only increased efficiency in producing desirable Reb D and Reb M but also transforms the landscape of low-calorie sweetening options!

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Playback language: English
Abstract
Steviol glycosides, intensely sweet components from *Stevia rebaudiana*, are potential low-calorie sweeteners. Reb D and Reb M, desirable for their lack of aftertaste, are naturally scarce. This study characterizes OsUGT91C1, a rice glycosyltransferase efficiently catalyzing β(1→2) glucosylation crucial for Reb D and Reb M synthesis. OsUGT91C1's flexibility stems from three substrate-binding modes, enabling β(1→2) glucosylation in two orientations and β(1→6) glucosylation. Engineered OsUGT91C1 variants enhance desired β(1→2) glucosylation, eliminate unwanted β(1→6) glucosylation, promising improved Reb D and Reb M production.
Publisher
Nature Communications
Published On
Dec 02, 2021
Authors
Jinzhu Zhang, Minghai Tang, Yujie Chen, Dan Ke, Jie Zhou, Xinyu Xu, Wenxian Yang, Jianxiong He, Haohao Dong, Yuquan Wei, James H. Naismith, Yi Lin, Xiaofeng Zhu, Wei Cheng
Tags
Steviol glycosides
OsUGT91C1
glycosyltransferase
Reb D
Reb M
β(1→2) glucosylation
sugar alternatives
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