scholarly journals Screening of an Endophyte Transforming Polydatin to Resveratrol from Reynoutria Japonica Houtt and the Optimization of Its Transformation Parameters

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4830
Author(s):  
Jin Liu ◽  
Xueqing Zhang ◽  
Ting Yan ◽  
Faling Wang ◽  
Jing Li ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Inhibitory Activity ◽  
High Performance ◽  
Ethyl Acetate Fraction ◽  
Reversed Phase ◽  
Transformation Rate ◽  
Inhibition Activity ◽  
Phylogenetic Tree Analysis ◽  
Glucose Content ◽  
Reynoutria Japonica

Resveratrol showed various kinds of bioactivities, such as antioxidant, antimicrobial, anticancer effects and, therefore, has been used widely as an important ingredient in medication, healthy foods and cosmetics. However, in nature, resveratrol usually exists at low content and more often exists as polydatin. Therefore, it becomes important to find the cost-effective and environmental-friendly way to transform polydatin to resveratrol. In this study, endophytes were isolated from the rhizome tissue of Reynoutria japonica and screened for transforming polydatin to resveratrol using reversed-phase high-performance liquid chromatography (RP-HPLC) and confirmed by liquid chromatography-mass spectrometry (LC-MS) and nuclear magnetic resonance (NMR) spectroscopy. A bacterium identified as Bacillus aryabhattai using 16S rRNA phylogenetic tree analysis showed highest transformation rate. The transforming conditions were optimized including substrate concentration, substrate addition time, culture temperature and inoculation ratio. Our results demonstrated that the bacteria isolated from R. japonica rhizome tissue showed high activity in transforming polydatin into resveratrol. Crude extract of R. japonica root and rhizome (RJE) was also tested as substrate and it was found that the transformation was significantly inhibited at 10.0 mg/mL RJE. Emodin at equivalent concentration of 10.0 mg/mL RJE showed no inhibition activity, and glucose content in RJE was trace and far from enough to exhibit the inhibitory activity. Successive solvent partition followed by an inhibition activity assay revealed that the ethyl acetate fraction showed the main inhibition activity. However, due to the coexistence of polydatin and compounds with inhibitory activity, the concentration of RJE can only be used at limited concentration as substrate.

Angiotensin I–Converting Enzyme Inhibitory Activity of Peptides Derived from Egg White Proteins by Enzymatic Hydrolysis

2004 ◽  
Vol 67 (9) ◽  
pp. 1914-1920 ◽  
Author(s):  
M. MIGUEL ◽  
I. RECIO ◽  
J. A. GÓMEZ-RUIZ ◽  
M. RAMOS ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
Inhibitory Activity ◽  
High Performance ◽  
Egg White ◽  
Reversed Phase ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

The hydrolysis of crude egg white with pepsin, trypsin, and chymotrypsin produced peptides with angiotensin-converting enzyme (ACE) inhibitory properties. These peptides were mainly derived from the proteolysis of ovalbumin. The most active hydrolysates were obtained after treatment with pepsin (50% inhibitory concentration [IC50], 55.3 μg/ml), with the fraction having a molecular mass lower than 3,000 Da giving the highest ACE inhibitory activity (IC50, 34.5 μg/ml). Nine subfractions were collected from the fraction with a molecular mass lower than 3,000 Da using semipreparative reversed-phase high-performance liquid chromatography. Considerable ACE inhibitory activity (IC50 < 40 μg/ml) was found in three of them. These subfractions were analyzed by reversed-phase high-performance liquid chromatography–tandem mass spectrometry, and 14 peptides were identified. These sequences were synthesized, and their ACE inhibitory activities were measured. Among the identified peptides, two novel sequences with potent ACE inhibitory activity were found. The amino acid sequences of these inhibitors were identified as Arg-Ala-Asp-His-Pro-Phe-Leu and Tyr-Ala-Glu-Glu-Arg-Tyr-Pro-Ile-Leu and showed IC50 values of 6.2 and 4.7 μM, respectively.

scholarly journals Dipeptidyl Peptidase-IV Inhibitory Activity and Related Molecular Mechanism of Bovine α-Lactalbumin-Derived Peptides

Molecules ◽  
2020 ◽  
Vol 25 (13) ◽  
pp. 3009
Author(s):  
Jing Gao ◽  
Han Gong ◽  
Xueying Mao
Keyword(s):  
Liquid Chromatography ◽  
Inhibitory Activity ◽  
High Performance ◽  
Gel Filtration ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Salt Bridges ◽  
Docking Analysis ◽  
Inhibitory Peptides ◽  
Dpp Iv

Identifying DPP-IV inhibitory peptides from dietary protein has attracted increased attention. In the present study, bovine α-lactalbumin hydrolysates were generated by alcalase for various hydrolysis times, and DPP-IV inhibitory activity of these hydrolysates was determined. The 4 h hydrolysates displayed the most potent DPP-IV inhibitory activity, with DPP-IV inhibition rate of 82.30 ± 1.39% at concentration of 1.0 mg/mL. DPP-IV inhibitory peptides were isolated from the 4 h-hydrolysates with gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). Using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI MS/MS), two DPP-IV inhibitory peptides were identified, and their amino acid sequences were Glu-Leu-Lys-Asp-Leu-Lys-Gly-Tyr (ELKDLKGY) and Ile-Leu-Asp-Lys-Val-Gly-Ile-Asn-Tyr (ILDKVGINY), respectively. Furthermore, molecular docking analysis showed that peptides ELKDLKGY and ILDKVGINY could form hydrogen bonds, pi-cation interactions, and salt bridges with DPP-IV. These findings indicated that bovine α-lactalbumin may be a potential source of natural DPP-IV inhibitor.

Development and Validation of A Reversed Phase-High Performance Liquid Chromatography Method for the Quantitative Estimation of Ramipril Drug Content from Formulated Dosage Form

2016 ◽  
Vol 6 (3) ◽  
Author(s):  
Raju Chandra ◽  
Manisha Pant ◽  
Harchan Singh ◽  
Deepak Kumar ◽  
Ashwani Sanghi
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Active Ingredient ◽  
High Performance ◽  
Limit Of Detection ◽  
Quantitative Estimation ◽  
Reversed Phase ◽  
Uv Detector ◽  
Chromatography Method ◽  
Drug Content

A reliable and reproducible reversed-phase high performance liquid chromatography (RP-HPLC) was developed for the quantitative determination of Remipril drug content from marketed bulk tablets. The active ingredient of Remipril separation achieved with C18 column using the methanol water mobile phase in the ratio of 40:60 (v/v). The active ingredient of the drug content quantify with UV detector at 215 nm. The retention time of Remipril is 5.63 min. A good linearity relation (R2=0.999) was obtained between drug concentration and average peak areas. The limit of detection and limit of quantification of the instrument were calculated 0.03 and 0.09 µg/mL, respectively. The accuracy of the method validation was determined 102.72% by recoveries method.

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