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1.
Food Chem Toxicol ; 121: 423-429, 2018 Nov.
Article in English | MEDLINE | ID: mdl-30172848

ABSTRACT

Orbignya speciosa and Mauritia flexuosa are two native palm tree species found in Brazil. Their fruits are rich in edible fixed oils, which are used for many purposes in industry, such as in the manufacture of soaps, surfactants and margarines. The aim of this work was to characterize the chemical profiles and antioxidant properties of the methanol extracts obtained from the fruits of O. speciosa and M. flexuosa. The chemical prospection was carried out using specific qualitative tests to evaluate the presence of phenolic compounds (tannins and flavonoids) in the extracts of both species. The antioxidant properties of the extracts were analyzed by the following methods: production of thiobarbituric acid reactive substances (TBARS) from phospholipids, deoxyribose degradation, radical-scavenging activity-DPPH, iron chelation assay and ferric-reducing antioxidant power (FRAP). The methanolic extracts obtained from M. flexuosa and O. speciosa presented significant antioxidant activities, although M. flexuosa presented higher antioxidant activity than O. speciosa. In conclusion, M. flexuosa and O. speciosa are important sources of antioxidant substances that may be useful in the development of new products to prevent diseases associated with oxidative stress.


Subject(s)
Antioxidants/pharmacology , Arecaceae/chemistry , Fruit/chemistry , Phytochemicals/chemistry , Antioxidants/chemistry , Biphenyl Compounds/chemistry , Free Radical Scavengers/chemistry , Free Radical Scavengers/pharmacology , Iron Chelating Agents , Phospholipids , Picrates/chemistry , Thiobarbituric Acid Reactive Substances
2.
Protein Pept Lett ; 18(4): 396-402, 2011 Apr.
Article in English | MEDLINE | ID: mdl-21121890

ABSTRACT

A new galactose-specific lectin, named BBL, was purified from seeds of Bauhinia bauhinioides by precipitation with ammonium sulfate, followed by two steps of ion exchange chromatography. BBL haemagglutinated rabbit erythrocytes (native and treated with proteolytic enzymes) showing stability even after exposure to 60 °C for an hour. The lectin haemagglutinating activity was optimum between pH 8.0 and 9.0 and inhibited after incubation with D-galactose and its derivatives, especially α-methyl-D-galactopyranoside. The pure protein possessed a molecular mass of 31 kDa by SDS-PAGE and 28.310 Da by mass spectrometry. The lectin pro-inflammatory activity was also evaluated. The s.c. injection of BBL into rats induced a dose-dependent paw edema, an effect that occurred via carbohydrate site interaction and was significantly reduced by L-NAME, suggesting an important participation of nitric oxide in the late phase of the edema. These findings indicate that BBL can be used as a tool to better understand the mechanisms involved in inflammatory responses.


Subject(s)
Bauhinia/chemistry , Plant Lectins/chemistry , Plant Lectins/isolation & purification , Animals , Edema/chemically induced , Erythrocytes/drug effects , Galactose/analogs & derivatives , Galactose/chemistry , Hemagglutinins/drug effects , Hemagglutinins/immunology , Male , NG-Nitroarginine Methyl Ester/pharmacology , Nitric Oxide/metabolism , Plant Lectins/pharmacology , Rabbits , Rats , Rats, Wistar , Seeds/chemistry
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