A α-L-rhamnosidase from Echinacea purpurea endophyte Simplicillium sinense EFF1 and its application in production of Calceorioside B

文献类型： 外文期刊

第一作者： Ban, Yali

作者： Ban, Yali;Yang, Hongwang;Jiang, Jixuan;Wang, Chengbin;Feng, Yongjun;Lv, Bo;Feng, Yongjun;Lv, Bo

作者机构：

关键词： Calceorioside B; Endophyte screening; alpha-L-Rhamnosidase; RNA -transcription; Enzymatic catalysis

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2024 年 270 卷

页码：

收录情况： SCI

摘要： Calceorioside B, a multifunctional phenylethanol glycosides (PhGs) derivative, exhibits a variety of notable properties, such as antithrombotic, anti-tumorigenic, anti-neocoronavirus, anti-inflammatory, and neuroprotective effects. However, the large-scale production of calceorioside B is routinely restricted by its existence as an intermediary compound derived from plants, and still unachieved through excellent and activity chemical synthesis. Here, a total of 51 fungal endophytes were isolated from four PhGs-producing plants, and endophyte Simplicillium sinense EFF1 from Echinacea purpurea was identified with the ability to de-rhamnosing isoacteoside to generate calceorioside B. According to the RNA-transcription of EFF1 under the various substrates, a key gene CL1206.Contig2 that undertakes the hydrolysis function was screened out and charactered by heterologous expression. The sequence alignment, phylogenetic tree construction and substrate specificity analysis revealed that CL1206 was a novel alpha-L-rhamnosidase that belongs to the glycosyl hydrolase family 78 (GH78). The optimum catalytic conditions for CL1206 were at pH 6.5 and 55 degrees C. Finally, the enzyme-catalyzed approach to produce calceorioside B from 50 % crude isoacteoside extract was explored and optimized, with the maximum conversion rate reaching 69.42 % and the average producing rate reaching 0.37 g-1.L-1.h- 1, which offered a great biocatalyst for potential industrial calceorioside B production. This is the first case for microorganism and rhamnosidase to show the hydrolysis ability to caffeic acid-modified PhGs.

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