Efficient bioconversion of epimedin C to icariin by a glycosidase from Aspergillus nidulans

Lyu, Yunbin; Zeng, Weizhu; Du, Guocheng; Chen, Jian; Zhou, Jingwen

doi:10.1016/j.biortech.2019.121612

Cited by 32 publications

(22 citation statements)

References 34 publications

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“…As the important factors affecting the enzyme-catalyzed reaction rate, the concentration of epimedin C, the amount of α-L-rhamnosidase, the reaction temperature, and the pH were studied for their effect on the yield of icariin and epimedin C remained. As shown in Figure 5 a, when the other reaction conditions were the same, the yield of icariin decreased as the concentration of epimedin C increased, which was similar to the previous study [ 14 ]. The biggest icariin yield in the reaction system containing 500 mg·L −1 epimedin C was 74.99 ± 0.42%, the value was 51.81 ± 6.56% and 26.67 ± 1.02% in the reaction system loaded 1000 mg·L −1 epimedin C and 1500 mg·L −1 epimedin C, respectively.…”

Section: Resultssupporting

confidence: 88%

“…When epimedin C was used as a nature substrate to determine the kinetic parameters of α-L-rhamnosidase, the values of K m and V max were 3.28 mM and 0.01 μmol·mg −1 ·min −1 , respectively ( Figure 3 g). K m of α-L-rhamnosidase with epimedin C as the substrate was higher than those of α-L-rhamnosidase from A. nidulans and T. petrophila [ 14 , 23 ].…”

Section: Resultsmentioning

confidence: 99%

“…The highest enzyme activity was set as 100%. To evaluate the temperature stability, the enzyme was kept in the citrate-phosphate buffer (200 mM, pH 7.0) at different temperatures (30, 35, 40, 45, 50, 55, 60, 65, and 70 °C) for various times (20, 40, 60, 80, and 120 min) [ 14 ]. Then, the enzyme activity was assayed as described in Section 2.4 .…”

Section: Methodsmentioning

confidence: 99%

“…α-L-rhamnosidase from Bacteroides thetaiotaomicron has the ability to transform epimedin C into icariin, and the bioconversion of epimedin C into icariin could reach 90.5% under the optimum conditions [ 13 ]. Identically, it was reported that recombinant Escherichia coli cells expressing α-L-rhamnosidase from Aspergillus nidulans could hydrolyze epimedium extracts to prepare icariin [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

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Purification and Characterization of a Novel α-L-Rhamnosidase from Papiliotrema laurentii ZJU-L07 and Its Application in Production of Icariin from Epimedin C

Lou

Liu

et al. 2022

JoF

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Icariin is the most effective bioactive compound in Herba Epimedii. To enhance the content of icariin in the epimedium water extract, a novel strain, Papiliotrema laurentii ZJU-L07, producing an intracellular α-L-rhamnosidase was isolated from the soil and mutagenized. The specific activity of α-L-rhamnosidase was 29.89 U·mg−1 through purification, and the molecular mass of the enzyme was 100 kDa, as assayed by SDS-PAGE. The characterization of the purified enzyme was determined. The optimal temperature and pH were 55 °C and 7.0, respectively. The enzyme was stable in the pH range 5.5–9.0 for 2 h over 80% and the temperature range 30–40 °C for 2 h more than 70%. The enzyme activity was inhibited by Ca2+, Fe2+, Cu2+, and Mg2+, especially Fe2+. The kinetic parameters of Km and Vmax were 1.38 mM and 24.64 μmol·mg−1·min−1 using pNPR as the substrate, respectively. When epimedin C was used as a nature substrate to determine the kinetic parameters of α-L-rhamnosidase, the values of Km and Vmax were 3.28 mM and 0.01 μmol·mg−1·min−1, respectively. The conditions of enzymatic hydrolysis were optimized through single factor experiments and response surface methodology. The icariin yield increased from 61% to over 83% after optimization. The enzymatic hydrolysis method could be used for the industrialized production of icariin. At the same time, this enzyme could also cleave the α-1,2 glycosidic linkage between glucoside and rhamnoside in naringin and neohesperidin, which could be applicable in other biotechnological processes.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification and Characterization of a Novel α-L-Rhamnosidase from Papiliotrema laurentii ZJU-L07 and Its Application in Production of Icariin from Epimedin C

Lou

Liu

et al. 2022

JoF

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“…Hemicelluloses can be hydrolyzed into pentoses (xylose and arabinose) and hexoses (glucose, mannose and galactose) at high yield which is important for bio-refinery applications [37,38]. Besides the enzymes degrading the main chains of the structural polysaccharides in plant cell walls, various glycosidases have been found to be essential for obtaining fermentable sugars from lignocellulose [39]. Glucosidase, xylosidase, and arabinofuranosidase played key roles in the production of glucose, xylose, and arabinose, respectively.…”

Section: Discussionmentioning

confidence: 99%

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

Zhang

Yang

Luo

et al. 2020

IJMS

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Fermentable sugars are important intermediate products in the conversion of lignocellulosic biomass to biofuels and other value-added bio-products. The main bottlenecks limiting the production of fermentable sugars from lignocellulosic biomass are the high cost and the low saccharification efficiency of degradation enzymes. Herein, we report the secretome of Trichoderma harzianum EM0925 under induction of lignocellulose. Numerously and quantitatively balanced cellulases and hemicellulases, especially high levels of glycosidases, could be secreted by T. harzianum EM0925. Compared with the commercial enzyme preparations, the T. harzianum EM0925 enzyme cocktail presented significantly higher lignocellulolytic enzyme activities and hydrolysis efficiency against lignocellulosic biomass. Moreover, 100% yields of glucose and xylose were obtained simultaneously from ultrafine grinding and alkali pretreated corn stover. These findings demonstrate a natural cellulases and hemicellulases mixture for complete conversion of biomass polysaccharide, suggesting T. harzianum EM0925 enzymes have great potential for industrial applications.

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Systematic Quality Evaluation of Epimedium wushanense T. S. Ying Based on Two Quality Control Standards: Total Flavonoid Glycosides and Epimedin C

wang

Tian

Tang

et al. 2023

Chemistry & Biodiversity

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Two quality control standards, total flavonoid glycosides of Epimedii Folium and epimedin C of Epimedii Wushanensis Folium, were used to systematically evaluate the quality of Epimedium wushanense T. S. Ying, so as to provide reference for its germplasm screening and resource utilization. Seven representative populations of E. wushanense covering its main distribution areas were uniformly sampled during the flowering period. There were significant quality differences among the populations of E. wushanense. According to the quality standard of total flavonoid glycosides, all populations were superior to the quality standard of the Chinese Pharmacopoeia for Epimedii Folium, with more than 1.5 % total flavonoid glycosides. The variation ranges of epimedin A, epimedin B, epimedin C, icariin and total flavonoid glycosides were 0.40–0.76 %, 0.51–0.83 %, 1.70–9.31 %, 0.40–1.23 % and 3.05–10.61 %, respectively. According to the quality standard of epimedin C, all populations were better than the quality standard of the Chinese Pharmacopoeia for Epimedii Wushanensis Folium, with more than 1.0 % epimedin C. The variation range of epimedin C was 2.22–10.06 %. When comparing the results of the two methods, a trend of slightly lower mean values was found for total flavonoid glycosides, except for the HBXW population. The quality of E. wushanense was superior to both the quality standard of Epimedii Folium and Epimedii Wushanense Folium in the Chinese Pharmacopoeia. Epimedin C was the most abundant component. Among the investigated populations, HBXW and HBGK exhibited the highest quality, and may provide excellent genetic resources for standardized cultivation. In addition, the habitat of these populations can also serve a reference for cultivation conditions.

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Efficient bioconversion of epimedin C to icariin by a glycosidase from Aspergillus nidulans

Cited by 32 publications

References 34 publications

Purification and Characterization of a Novel α-L-Rhamnosidase from Papiliotrema laurentii ZJU-L07 and Its Application in Production of Icariin from Epimedin C

Purification and Characterization of a Novel α-L-Rhamnosidase from Papiliotrema laurentii ZJU-L07 and Its Application in Production of Icariin from Epimedin C

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

Systematic Quality Evaluation of Epimedium wushanense T. S. Ying Based on Two Quality Control Standards: Total Flavonoid Glycosides and Epimedin C

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