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1.
Int J Mol Sci ; 24(18)2023 Sep 12.
Article in English | MEDLINE | ID: mdl-37762289

ABSTRACT

Dairy protein hydrolysates possess a broad spectrum of bioactivity and hypoallergenic properties, as well as pronounced bitter taste. The bitterness is reduced by complexing the proteolysis products with cyclodextrins (CDs), and it is also important to study the bioactivity of the peptides in inclusion complexes. Hydrolysates of whey and colostrum proteins with extensive hydrolysis degree and their complexes with ß/γ-CD were obtained in the present study, and comprehensive comparative analysis of the experimental samples was performed. The interaction of CD with peptides was confirmed via different methods. Bioactivity of the initial hydrolysates and their complexes were evaluated. Antioxidant activity (AOA) was determined by fluorescence reduction of fluorescein in the Fenton system. Antigenic properties were studied by competitive enzyme immunoassay. Antimutagenic effect was estimated in the Ames test. According to the experimental data, a 2.17/2.78-fold and 1.45/2.14-fold increase in the AOA was found in the ß/γ-CD interaction with whey and colostrum hydrolysates, respectively. A 5.6/5.3-fold decrease in the antigenicity of whey peptides in complex with ß/γ-CD was detected, while the antimutagenic effect in the host-guest systems was comparable to the initial hydrolysates. Thus, bioactive CD complexes with dairy peptides were obtained. Complexes are applicable as a component of specialized foods (sports, diet).


Subject(s)
Antimutagenic Agents , gamma-Cyclodextrins , Female , Pregnancy , Humans , Whey , Colostrum , Whey Proteins/pharmacology , Peptides/pharmacology
2.
Molecules ; 27(3)2022 Jan 24.
Article in English | MEDLINE | ID: mdl-35164026

ABSTRACT

Chlorophytum genus has been extensively studied due to its diverse biological activities. We evaluated the methanolic extract of leaves of Chlorophytum comosum (Green type) (Thunb.) Jacques, the species that is less studied compared to C. borivilianum. The aim was to identify phytoconstituents of the methanolic extract of leaves of C. comosum and biological properties of its different fractions. Water fraction was analyzed with matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. Nineteen compounds belonging to different chemical classes were identified in the methanolic extract of leaves of C. comosum (Green type) (Thunb.) Jacques. In addition to several fatty acids, isoprenoid and steroid compounds were found among the most abundant constituents. One of the identified compounds, 4'-methylphenyl-1C-sulfonyl-ß-d-galactoside, was not detected earlier in Chlorophytum extracts. The water fraction was toxic to HeLa cells but not to Vero cells. Our data demonstrate that methanolic extract of leaves of C. comosum can be a valuable source of bioactive constituents. The water fraction of the extract exhibited promising antitumor potential based on a high ratio of HeLa vs. Vero cytotoxicity.


Subject(s)
Asparagaceae/chemistry , Plant Extracts/pharmacology , Animals , Antioxidants/chemistry , Cell Survival/drug effects , Chemical Fractionation , Chlorocebus aethiops , Gas Chromatography-Mass Spectrometry , HeLa Cells , Humans , Methanol/chemistry , Phytochemicals/chemistry , Plant Extracts/chemistry , Plant Leaves/chemistry , Toxicity Tests , Vero Cells
3.
Biochem Biophys Res Commun ; 342(2): 459-64, 2006 Apr 07.
Article in English | MEDLINE | ID: mdl-16487485

ABSTRACT

The ability of a number of hemeproteins to oxidize the flavonoid quercetin has been shown. It was found that quercetin undergoes chemical modification in the presence of cytochrome c, myoglobin, and hemoglobin but not cytochrome b(5). In the range of investigated proteins the most effective oxidant appears to be cytochrome c. Chromatographic analysis of the reaction mixture revealed a number of quercetin oxidation products. The main oxidation product was purified and characterized by means of LC-MS and NMR analyses. It has a dimeric structure similar to the product of quercetin oxidation by horseradish peroxidase and is formed during radical-driven reactions. Our results indicate that a number of hemeproteins can react and modify biologically active flavonoids. However, these reactions might also lead to the generation of active species with deleterious consequences for the cellular macromolecules.


Subject(s)
Hemeproteins/chemistry , Hemeproteins/metabolism , Quercetin/chemistry , Quercetin/metabolism , Animals , Chromatography, Liquid , Cytochromes c/chemistry , Cytochromes c/metabolism , Flavonoids/chemistry , Flavonoids/metabolism , Horses , Kinetics , Magnetic Resonance Spectroscopy , Mass Spectrometry , Oxidants/chemistry , Oxidants/metabolism , Oxidation-Reduction , Spectrophotometry, Ultraviolet
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