529-55-5

Usage

Uses

Used in Pharmaceutical Applications:
Naringenin-7-O-glucoside is used as a bioactive compound for its tyrosine phosphatase 1B inhibition and stimulation of glucose uptake in insulin-resistant HepG2 cells. This makes it a promising candidate for the development of drugs targeting type 2 diabetes and related metabolic disorders.
Used in Functional Foods and Nutraceuticals:
Naringenin-7-O-glucoside is used as an ingredient in functional foods and nutraceuticals for its potential health benefits, including its antioxidant and anti-inflammatory properties. It may contribute to the development of products aimed at promoting overall health and well-being.
Used in Cosmetics:
In the cosmetics industry, Naringenin-7-O-glucoside is used as an active ingredient for its antioxidant and anti-inflammatory properties. It may be incorporated into skincare products to help protect the skin from environmental stressors and promote a healthy, youthful appearance.
Used in Agricultural Applications:
Naringenin-7-O-glucoside may also be used in agricultural applications, particularly in the development of plant-derived products with enhanced nutritional and health-promoting properties. Its bioactive properties could be harnessed to improve the quality and value of crops and derived products.

Upstream product

• 10236-47-2 naringin 
• 64-18-6 formic acid 
• 108-93-0 cyclohexanol 
• 94392-49-1 naringenin 7-O-(6-O-((E)-p-coumaroyl)-β-D-glucopyranoside) 
• 480-41-1 naringenin 
• 480-41-1 5,7-Dihydroxy-2-(4-hydroxy-phenyl)-chroman-4-on 
• 133-89-1 UDP-glucose 

Downstream Products

• 492-62-6 alpha-D-glucopyranose 
• 480-41-1 naringenin 
• 1256627-52-7 prunin 6''-O-stearate 
• 1256627-53-8 prunin 6''-O-laurate 
• 1256627-51-6 prunin 6''-O-decanoate 
• 1256627-50-5 prunin 6''-O-butyrate 
• 252324-55-3 prunin 6''-O-acetate 
• 491-69-0 (2S)-poncirenin 

Relevant academic research and scientific papers

Covalent Immobilization of Naringinase over Two-Dimensional 2D Zeolites and its Applications in a Continuous Process to Produce Citrus Flavonoids and for Debittering of Juices

The crude naringinase from Penicillium decumbens and a purified naringinase with high α-L-rhamnosidase activity could be covalently immobilized on two-dimensional zeolite ITQ-2 after surface modification with glutaraldehyde. The influence of pH and temperature on the enzyme activity (in free and immobilized forms) as well as the thermal stability were determined using the specific substrate: p-nitrophenyl-alpha-L-rhamnopyranoside (Rha-pNP). The crude and purified naringinase supported on ITQ-2 were applied in the hydrolysis of naringin, giving the flavonoids naringenin and prunin respectively with a conversion '90 percent and excellent selectivity. The supported enzymes showed long term stability, being possible to perform up to 25 consecutive cycles without loss of activity, showing its high potential to produce the valuable citrus flavonoids prunin and naringenin. We have also succeeded in the application of the immobilized crude naringinase on ITQ-2 for debittering grapefruit juices in a continuous process that was maintained operating for 300 h, with excellent results.

Two trifunctional leloir glycosyltransferases as biocatalysts for natural products glycodiversification

Two promiscuous Bacillus licheniformis glycosyltransferases, YdhE and YojK, exhibited prominent stereospecific but nonregiospecific glycosylation activity of 20 different classes of 59 structurally different natural and non-natural products. Both enzymes transferred various sugars at three nucleophilic groups (OH, NH2, SH) of diverse compounds to produce O-, N-, and S-glycosides. The enzymes also displayed a catalytic reversibility potential for a one-pot transglycosylation, thus bestowing a cost-effective application in biosynthesis of glycodiversified natural products in drug discovery.

Regioselective O-glycosylation of flavonoids by fungi Beauveria bassiana, Absidia coerulea and Absidia glauca

In the present study, the species: Beauveria bassiana, Absidia coerulea and Absidia glauca were used in biotransformation of flavones (chrysin, apigenin, luteolin, diosmetin) and flavanones (pinocembrin, naringenin, eriodictyol, hesperetin). The Beauveria bassiana AM 278 strain catalyzed the methylglucose attachment reactions to the flavonoid molecule at positions C7 and C3′. The application of the Absidia genus (A. coerulea AM 93, A. glauca AM 177) as the biocatalyst resulted in the formation of glucosides with a sugar molecule present at C7 and C3′ positions of flavonoids skeleton. Nine of obtained products have not been previously reported in the literature.

An alkali tolerant α-L-rhamnosidase from Fusarium moniliforme MTCC-2088 used in de-rhamnosylation of natural glycosides

Analkali tolerant α-L-rhamnosidase has been purified to homogeneity from the culture filtrate of a new fungal strain, Fusarium moniliforme MTCC-2088, using concentration by ultrafiltration and cation exchange chromatography on CM cellulose column. The molecular mass of the purified enzyme has been found to be 36.0 kDa using SDS-PAGE analysis. The Km value using p-nitrophenyl-α-L-rhamnopyranoside as the variable substrate in 0.2 M sodium phosphate buffer pH10.5 at50 °C was 0.50 mM. The catalytic rate constant was15.6 s?1giving the values of kcat/Km is 3.12 × 104M?1 s?1. The pH and temperature optima of the enzyme were 10.5 and 50 °C, respectively. The purified enzyme had better stability at 10 °C in basic pH medium. The enzyme derhamnosylated natural glycosides like naringin to prunin, rutin to isoquercitrin and hesperidin to hesperetin glucoside. The purified α-L-rhamnosidase has potential for enhancement of wine aroma.

Purification and characterization of an intracellular α-L-rhamnosidase from a newly isolated strain, Alternaria alternata SK37.001

A strain, Alternaria alternata SK37.001, which produces an intracellular α-L-rhamnosidase, was newly isolated from citrus orchard soil. The molecular mass of the enzyme was 66 kDa, as evaluated by SDS-PAGE and 135 kDa, as determined by gel filtration, which indicated that the enzyme is a dimer. The enzyme had a specific activity of 21.7 U mg?1 after step-by-step purification. The optimal pH and temperature were 5.5 and 60 °C, respectively. The enzyme was relatively stable at a pH of 4.0–8.0 and a temperature between 30 and 50 °C compared with other pH levels and temperatures investigated. The enzyme activity was accelerated by Ba2+ and Al3+ but inhibited by Ni2+, Cu2+ and Co2+, especially Ni2+. The kinetic parameters of Km and Vmax were 4.84 mM and 53.1 μmol mg?1 min?1, respectively. The α-L-rhamnosidase could hydrolyze quercitrin, naringin and neohesperidin, hesperidin and rutin rhamnose-containing glycosides but could not hydrolyze ginsenoside Rg2 or saiko-saponin C.

Preparation of Prunin and derivative thereof and application of Prunin derivative in drugs for relieving cough and reducing phlegm

The invention relates to preparation of a Prunin derivative and application thereof in drugs for relieving a cough and reducing phlegm. The Prunin derivative is obtained by introducing glycosyl or aliphatic chains or an amine group or an ether group, and the water solubility, the dissolving-out speed and the bioavailability are significantly improved. The Prunin derivative has better cough relieving and phlegm reducing effects, the curative effects on various coughs and asthma caused by acute bronchitis, chronic bronchitis, colds and the like are significant, and no toxic or side effect exists; compared with traditional cough medicine Nin Jiom Pei Pa Koa, the curative effect is more significant, and the Prunin derivative is an ideal drug for relieving the cough and reducing the phlegm, andhas a wide market prospect. The formula is defined in the description.

Preparation method of flavone aglycone or monoglycoside from aluminum-salt-flavonoid-glycoside complex through hydrolysis

Disclosed is a preparation method of flavone aglycone or monoglycoside from aluminum-salt-flavonoid-glycoside complex through hydrolysis. The problems that flavonoid glycosides neither dissolve in water nor are hard to dissolve in a common organic alcohol solution, and flavone aglycone prepared from hydrolysis has slow hydrolysis speed, needs a large amount of an organic solvent, and cannot be totally hydrolyzed are solved. A complex product from complexation of aluminum salt and flavonoid glycosides is easy to dissolve in alcohol, hydrogen chloride generated by the complex product is utilized with addition of hydrochloric acid or sulfuric acid, and hydrolysis is carried out at a certain temperature to prepare aglycone or a mixture of aglycone and monoglycoside. After the reaction is over, phosphoric acid or phosphate is added to break complexation of aluminum ions and flavone to obtain flavone aglycone, or the mixture of flavone aglycone and flavone monoglycoside, or a mixture of flavone aglycone, flavone monoglycoside, and flavonoid glycoside. The method is simple and easy to operate, relatively high in yield and purity, and extremely low in cost, and is suitable for massive industrial production of flavone aglycone or the mixture of flavone aglycone and flavone monoglycoside.

α-Rhamnosidase activity in the marine isolate Novosphingobium sp. PP1Y and its use in the bioconversion of flavonoids

Crude protein extracts of Novosphingobium sp. PP1Y, a microorganism isolated from polluted marine waters in Pozzuoli (Italy), were analyzed for the presence of glycosidase activities. Particular attention was devoted to a α-L-rhamnosidase activity able to hydrolyze several flavonoids of interest for the pharmaceutical and food industries. This activity had an alkaline pH optimum and a moderate tolerance to the presence of organic solvents, appealing features for its possible biotechnological uses. An increase of the α-L-rhamnosidase activity in PP1Y crude extracts was induced by adding naringin to the growth medium, suggesting the possibility to use material from Citrus industrial waste to induce the glycosidase activity expressed by strain PP1Y and produce simultaneously high-added-value molecules from the hydrolysis of their flavonoids. In order to investigate on the enzymatic mechanism of PP1Y α-L-rhamnosidase activity, hydrolysis products of PNP-α-L- rhamnopyranoside were analyzed by 1H-NMR experiments. The kinetic behaviour clearly indicated an inverting mechanism of hydrolysis for this novel enzymatic activity.

Purification and characterization of a naringinase from Aspergillus aculeatus JMUdb058

A naringinase from Aspergillus aculeatus JMUdb058 was purified, identified, and characterized. This naringinase had a molecular mass (MW) of 348 kDa and contained four subunits with MWs of 100, 95, 84, and 69 kDa. Mass spectrometric analysis revealed that the three larger subunits were β-d-glucosidases and that the smallest subunit was an α-l-rhamnosidase. The naringinase and its α-l-rhamnosidase and β-d-glucosidase subunits all had optimal activities at approximately pH 4 and 50 C, and they were stable between pH 3 and 6 and below 50 C. This naringinase was able to hydrolyze naringin, aesculin, and some other glycosides. The enzyme complex had a Km value of 0.11 mM and a kcat/Km ratio of 14 034 s-1 mM -1 for total naringinase. Its α-l-rhamnosidase and β-d-glucosidase subunits had Km values of 0.23 and 0.53 mM, respectively, and kcat/Km ratios of 14 146 and 7733 s -1 mM-1, respectively. These results provide in-depth insight into the structure of the naringinase complex and the hydrolyses of naringin and other glycosides.

Pressure-enhanced activity and stability of α-l-rhamnosidase and β-d-glucosidase activities expressed by naringinase

Naringinase is an enzyme complex, expressing α-l-rhamnosidase and β-d-glucosidase activities. The impact of high pressure and temperature on naringinase activity and stability were studied, in order to assess the potential of enzyme thermostability on glycosides hydrolyses. To a better understanding of these effects on naringinase enzyme complex, they were also evaluated over α-l-rhamnosidase and β-d-glucosidase activities, using specific substrates, p-nitrophenyl α-l-rhamnopyranoside (4-NRham) and p-nitrophenyl β-d-glucopyranoside (4-NGluc), respectively. Hydrolysis rate of 4-NRham and naringin increased with pressure from 0.1 to 150 MPa. The equilibrium constants for α-l-rhamnosidase and β-d-glucosidase reactions, at pressures of 0.1-200 MPa and 40 °C, were determined and best fitted with the model of Baliga and Whalley equation. Accordingly, reaction volumes of 93 and 64 mL mol-1 were obtained for α-l-rhamnosidase and β-d-glucosidase reactions, respectively. Reaction rate constants were also determined at the same experimental conditions and well fitted to the models of Golinkin, Laidlaw, Hyne and of Burris and Laidler. A negative ΔV≠ of -7.7 ± 1.5 and -20.0 ± 5.2 mL mol-1 were obtained for α-l-rhamnosidase and naringinase reactions, correspondingly, which reflect the accelerating effect of pressure on the biocatalysis. Moreover, the KM, kcat and kcat/KM values, on naringin hydrolysis under atmospheric (0.1 MPa) and high pressure (150 MPa) conditions at different temperatures (25-80 °C) were determined. A 3-fold and 4-fold increase on naringinase thermostability was observed under 150 MPa at 70 and 80 °C, respectively, compared to 0.1 MPa experiments. In addition, a 15-fold increase of kcat/kM values from experimental conditions of 0.1 MPa and 30 °C to 150 MPa and 70 °C was observed. In fact, high pressure showed to be a powerful tool to increase stability of naringinase against thermal denaturation. In conclusion, the effect of amplification of pressure effects on reaction rates by temperature could have a pragmatic use for accelerating enzymatic reactions.