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High-efficiency flavonoid deglycosylation of whole cells with surface display of α-L-rhamnosidase in Escherichia coli

文献类型： 外文期刊

作者： Yan, Cheng-Hai 1 ; Wang, Ding 3 ; Mei, Ruo-Xi 1 ; Tan, Lu 1 ; Li, Yi-Jiang-Cheng 1 ; Herman, Richard Ansah 1 ; Xu, Yan 1 ; Gong, Lu-Chan 1 ; Wang, Jun 1 ;

作者机构： 1.Jiangsu Univ Sci & Technol, Sch Biotechnol, Jiangsu Key Lab Sericultural & Anim Biotechnol, Zhenjiang 212100, Jiangsu, Peoples R China

2.Chinese Acad Agr Sci, Sericultural Sci Res Ctr, Key Lab Silkworm & Mulberry Genet Improvement, Minist Agr & Rural Affairs, Zhenjiang 212100, Jiangsu, Peoples R China

3.Jiangsu Univ Technol, Joint Lab Synthet Biol & Intelligent Biomfg, Changzhou 213001, Jiangsu, Peoples R China

关键词： alpha-L-rhamnosidase; Deglycosylation; Flavonoid; Surface display; Whole-cell catalyst

期刊名称：FOOD BIOSCIENCE （ 影响因子：5.9； 五年影响因子：6.1 ）

ISSN： 2212-4292

年卷期： 2025 年 65 卷

页码：

收录情况： SCI

摘要： Natural flavonoids exhibit diverse physiological effects and are used as functional factors, antioxidants and pigments in food as well as pharmaceutical and cosmetic applications. However, their poor solubility and stability, result in low bioavailability. Biomodification through deglycosylation effectively enhances their bioactivity. This study developed two surface display strategies in Escherichia coli, anchoring alpha-L-rhamnosidase RhaB1-Delta N to the cell surface using the anchoring protein Lpp-OmpA. Immunofluorescence and proteinase K sensitivity tests confirmed the successful construction of surface-displaying strains E. coli Lpp-OmpA-RhaB1-Delta N and E. coli Lpp-OmpA-SpyCatcher/RhaB1-Delta N-SpyTag. Enzymatic property studies revealed improved temperature and pH stability of the whole-cell catalysts with surface compared to free enzymes. After 6 catalytic cycles, E. coli Lpp-OmpA-RhaB1-Delta N retained higher activity than E. coli RhaB1-Delta N. In flavonoid hydrolysis, E. coli Lpp-OmpA-RhaB1-Delta N increased yields of isoquercitrin and kaempferol-3-O-glucuronide by 20.25% and 10.99%, respectively, compared with that in whole-cell catalyst with intracellular enzyme (p < 0.05). In addition, it should be noted that although the enzyme expression of E. coli Lpp-OmpA-SpyCatcher/RhaB1-Delta N-SpyTag is reduced, its hydrolysis ability of flavonoids is comparable to that of E. coli RhaB1-Delta N due to the efficient catalytic ability of extracellular enzymes. This study establishes reliable whole-cell catalysts with surface-displayed alpha-L-rhamnosidase for efficient natural flavonoid modification, with potential applications in the food and pharmaceutical industries.

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