Related Experiment Video
Updated: Mar 2, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Molecular cloning and expression of a glycosyltransferase from Bacillus subtilis for modification of morin and
Qianqian Wang1,2, Yixiang Xu3, Jiaqi Xu2
1State Key Laboratory of Natural Medicines, China Pharmaceutical University, 24# TongJia Xiang Street, Nanjing, 210009, Jiangsu, China.
Objectives:
To characterize glycosyltransferases from Bacillus subtilis ATCC 6633 and investigate their substrate specificity towards plant polyphenols.
Results:
Among the cloned and expressed six UDP-glycosyltransferases (BsGT1-6), BsGT-1 showed activity with a wide range of polyphenols: morin, quercetin, alizarin, rehin, curcumin and aloe emodin. The gene of BsGT-1 has an ORF of 1206 bp encoding 402 amino acids. The recombinant enzyme was purified to homogeneity by Ni-NTA affinity chromatograph, and its biochemical characteristics were identified by HPLC-UV/MS, 1H-NMR and 13C-NMR. BsGT-1 has an MW of approx. 46 kDa as indicated by SDS-PAGE; its activity was optimal at 40 °C and pH 8.5. The Km value of BsGT-1 towards morin was 110 μM.
Conclusions:
BsGT-1 from B. subtilis was cloned. It had high catalytic capabilities towards polyphenols which would make it feasible for the structural modification of polyphenols.

