Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates

The objective of this study was to identify the angiotensin I-converting enzyme (ACE)-inhibitory peptides released from thermally treated Phaseolus vulgaris (pinto) whole beans after in vitro gastrointestinal digestion. The degree of hydrolysis increased during digestion reaching a value of 50% at the end of the pancreatic digestion. The <3 kDa fraction of the postpancreatic sample showed high ACE-inhibitory activity (IC50 = 105.6 ± 2.1 μg of peptides/mL). Peptides responsible for the ACE-inhibitory activity were isolated by reverse-phase high-performance liquid chromatography (HPLC). Three fractions, showing the highest inhibitory activity, were selected for tandem mass spectrometry (MS/MS) experiments. Eleven of the identified sequences have previously been described as ACE-inhibitors. Most of the identified bioactive peptides have a hydrophobic amino acid, (iso)leucine or phenylalanine, or proline at the C-terminal position, which is crucial for their ACE-inhibitory activity. The sequence of some peptides allowed us to anticipate the presence of ACE-inhibitory activity.

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“…The total protein extract from pinto beans whole seeds was prepared according to Carrasco-Castilla et al, (2012).…”

Section: Determination Of the Degree Of Hydrolysismentioning

confidence: 99%

“…Samples taken at different times of digestion were subjected to SDS-PAGE electrophoresis using 13% polyacrylamide separating gel according to Carrasco-Castilla et al (2012). Samples were diluted to similar end dilutions in Laemmli buffer (0.05 mol/L Tris, pH 6.8, containing 2% SDS, 0.1 mol/L DTT and 0.025% bromophenol blue).…”

Section: Sds-page Electrophoresismentioning

confidence: 99%

Identification of ACE-inhibitory peptides fromPhaseolus vulgarisafterin vitrogastrointestinal digestion

Tagliazucchi

Martini

Bellesia

et al. 2015

International Journal of Food Sciences and Nutrition

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“…Moreover, the emission spectrum of intrinsic fluorescence of EH was indicative of changes at the level of the tertiary structure of the protein, as well as the exposure at aqueous phase of sequences with one or more amino acid residues of His, Trp, Tyr, Met, Pro, Leu, Ile, Val and Ala (Adebiyi et al, 2009). These amino acids donate protons/electrons to the deficient radicals to maintain the stability of molecular electron resonance structure, as occurs in antioxidant activity of hydrolysates of Glycine max in liposomal systems (Peña-Ramos & Xiong, 2002) and peptide fractions of Phaseolus vulgaris (Carrasco-Castilla et al, 2012).…”

Section: Antioxidant Activitymentioning

confidence: 99%

Effects of sequential enzymatic hydrolysis on structural, bioactive and functional properties of Phaseolus lunatus protein isolate

et al. 2014

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“…Catalase activity in 1.5 mg/kg dose is lowest than any other, being this probably due to a prooxidant effect of lectins at high doses, according to Carrasco-Castilla et al in 2012 [39]. Catalase activity is higher at 1.0 mg/kg and 1.0 mg/kg + NiO doses, this could be considered the best dose evaluated in this paper.…”

Section: Discussionmentioning

confidence: 60%

“…Lectin antioxidant activity has been evaluated and determined that it tends to be exposure-response relationship [40], but other authors suggest to consider also the possibility of a synergic activity between lectins and other plant metabolites [41] and even propose that the antioxidant activity is via iron and copper chelation [42], avoiding that those molecules bind to others and maximize oxidative stress; or even that lectins could have a prooxidant effect against other proteins of the same plant [42].…”

Section: Discussionmentioning

confidence: 99%

Oxidative Stress Evaluation in Cancer-Induced Mice Treated with Ruta graveolens L. Stem lectins

Torres-Alvarez¹,

Mendoza-Vallejo²,

Machuca-Rodríguez³

2015

JLS

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Abstract:The production of free radicals is a natural process in aerobic organisms due to the mitochondrial activity. Usually the cells have several mechanisms for scavenging those free radicals, but, in several pathologic processes, such as cancer, those free radicals increase their production, making it impossible to sustain the system stable, generating the condition called oxidative stress. Ruta graveolens L. (Rue) is a plant commonly used in traditional medicine, mainly as antiinflamatory; this has been related to some organic components, such as Rutin, but there hasn't been any lectin studies in Rue stem. Lectins are glycoproteins of non-enzymatic and no immune origin, able to bind to simple carbohydrates, which lets them bind selectively to malignant cells against normal cells, killing them via apoptosis and reducing the free radicals level. In this study we intended to characterize rue stem lectins as those weren't reported yet. Also, the anticancer and antioxidant activity of these lectins was evaluated, Rue stem lectins were extracted using a saline solution and semipurified to obtain an enriched extract and administrated to nickel oxide treated mice. Oxidative stress was cuantified using the tiobarbituric acid (TBARS) method to quantify Malondialdehyde (MDA), the Griess method to cuantify Nitrites and enzymatic activity of catalase were cuantified in liver. In this study was found that rue stem lectins are useful as a therapeutic auxiliar, considering that its ratio of antioxidant activity is limited, being a prooxidant agent at high concentrations.

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Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates

Cited by 143 publications

References 28 publications

Identification of ACE-inhibitory peptides fromPhaseolus vulgarisafterin vitrogastrointestinal digestion

Identification of ACE-inhibitory peptides fromPhaseolus vulgarisafterin vitrogastrointestinal digestion

Effects of sequential enzymatic hydrolysis on structural, bioactive and functional properties of Phaseolus lunatus protein isolate

Oxidative Stress Evaluation in Cancer-Induced Mice Treated with Ruta graveolens L. Stem lectins

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