Identification of a Novel Glycosyltransferase CaUGT Specifically Targeting the C-30 Position of Glycyrrhetinic Acid and Development of an Efficient Enzymatic Biotransformation System.

Authors

Daiyi Zheng, Wenxuan Tao, Yucheng Zhang, Xianying Fang, Jianjun Pei, Qi Li, Linguo Zhao

Published in

Journal of agricultural and food chemistry. Jul 08, 2026. Epub Jul 08, 2026.

Abstract

Glycyrrhetinic acid (GA) is a major bioactive ingredient of licorice with extensive pharmacological functions, while its strong hydrophobicity and low permeability severely restrict practical application. Enzymatic glycosylation serves as a mild method to enhance GA solubility and bioactivity, yet few reported glycosyltransferases can specifically modify the C30 carboxyl group of GA. In this study, a novel glycosyltransferase gene CaUGT was identified and cloned from Cardamine amara subsp. amara. The recombinant GST-CaUGT achieved optimal expression under 2% dextrin, 0.2 mM IPTG and 25 °C induction temperature. The enzyme exhibited the highest activity at 25 °C and pH 6.0, with high thermal and pH stability. It displayed a strict regioselectivity toward the GA C30 carboxyl, with a K_m of 0.0501 mmol/L and a k_cat of 52.3 s^-1·M^-1. A constructed two-enzyme cascade system produced 452.8 mg/L GA 30-O-glucoside with a space-time yield of 600.9 mg/L/h, providing an efficient biocatalytic route for triterpenoid carboxyl glycosylation.

PMID:
42418701
Bibliographic data and abstract were imported from PubMed on 09 Jul 2026.

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