Common bean (Phaseolus vulgaris L.) hydrolysates inhibit inflammation in LPS-induced macrophages through suppression of NF-κB pathways

Oseguera‐Toledo, Miguel E.; Mejía, Elvira González de; Dia, Vermont P.; Amaya-Llano, Silvia L.

doi:10.1016/j.foodchem.2011.01.121

Cited by 88 publications

(56 citation statements)

References 31 publications

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“…Our results indicate that phaseolin was susceptible to Alcalase and Savinase action probably due to their (continued on next page) broad specificity. Susceptibility of phaseolin to Alcalase and other proteases has also been reported by other authors (Oseguera-Toledo et al, 2011;Rui, Boye, Simpson, & Prasher, 2012). Nevertheless, there is a clear variability in the proteolytic rate of phaseolin by Alcalase among different studies.…”

Section: Discussionsupporting

confidence: 70%

Simultaneous release of peptides and phenolics with antioxidant, ACE-inhibitory and anti-inflammatory activities from pinto bean (Phaseolus vulgaris L. var. pinto) proteins by subtilisins

García-Mora

Frı́as

Peñas

et al. 2015

Journal of Functional Foods

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Available online A B S T R A C TProduction of novel functional ingredients from legume proteins is a valuable strategy to boost their food use and intake. Aimed at a better exploitation of the functional properties of pinto bean hydrolysates, the effectiveness of two subtilisins (Alcalase and Savinase) for the simultaneous release of bioactive peptides and phenolics with antioxidant, angiotensin I converting enzyme (ACE) inhibitory and anti-inflammatory activities was investigated.A higher proteolytic efficiency was observed for Alcalase that increased the concentration of small peptides in hydrolysates after 120 min. Savinase improved hydroxycinnamic acids and flavonoid contents in hydrolysates after 90 min due to its higher esterase activity. The most active hydrolysates combined potent free radical scavenging (326-348 mmol TE/g), ACE inhibitory (IC50 = 0.22-0.26 mg/mL) and anti-inflammatory (28-16% inhibition) activities. Peptide characterization of active hydrolysates confirmed the presence of bioactive fragments derived from phaseolin. These results evidence the promising potential of pinto bean hydrolysates as functional ingredients in the design of healthy foods.

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Section: Discussionsupporting

confidence: 70%

Simultaneous release of peptides and phenolics with antioxidant, ACE-inhibitory and anti-inflammatory activities from pinto bean (Phaseolus vulgaris L. var. pinto) proteins by subtilisins

García-Mora

Frı́as

Peñas

et al. 2015

Journal of Functional Foods

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show abstract

“…Oseguera-Toledo et al (2011) also performed alcalase hydrolysis of common bean proteins and found that phaseolin, was slowly hydrolyzed, until complete degradation after 3 h. Alcalase hydrolysis resulted in the breakdown of the phaseolin structure for all bean samples, independently of germination time (Fig. 1B, b) starting right after 1 h of hydrolysis.…”

Section: Sds-page Electrophoretic Profilementioning

confidence: 93%

Germination of Phaseolus vulgaris and alcalase hydrolysis of its proteins produced bioactive peptides capable of improving markers related to type-2 diabetes in vitro

Rocha

Hernandez

Mojica

et al. 2015

Food Research International

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The aim of this study was to evaluate the effect of germination and alcalase hydrolysis of common bean proteins on the generation of bioactive peptides with potential to reduce parameters related to the risk of developing type-2 diabetes (T2D) in vitro. Germination (25°C up to 72 h) and alcalase hydrolysis (up to 4 h) produced peptides with high antioxidant capacity (1085 μmol TE/g soluble protein, SP). After 24 h of germination, there was an increase of 44% in α-amylase inhibitory capacity of the peptides relative to acarbose (1 mM). Simulated gastrointestinal digestion of the non-germinated and non-hydrolyzed sample (G0-0h) produced bioactive peptides that inhibited dipeptidyl peptidase-IV (DPP-IV) (IC 50 = 1.2 mg SP/mL); however, the IC 50 was not improved by either germination or alcalase hydrolysis. Insulin secretion by glucose stimulated (20 mM) INS-1E pancreatic β-cells, increased 45% from the basal state with 2 mg SP/mL of G0-0h. Germination did not improve the stimulation of insulin. Computational modeling showed that the peptide RGPLVNPDPKPFL obtained after 48 h germination and 1 h alcalasehydrolysis was able to inhibit DPP-IV by interacting with its S1, S2, and S3 pockets of the active site. Germination and alcalase hydrolysis can be applied to improve some markers related to the management of T2D. Furthermore, simulated gastrointestinal digestion of common bean proteins without any treatment produced bioactive peptides with the ability to inhibit DPP-IV, resulting in increased insulin released from pancreatic cells in vitro.

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“…Complete hydrolysates and <1 kDa fractions were further subjected to simulated gastrointestinal digestion using pepsin-pancreatin (Oseguera-Toledo et al, 2011). A consistent increase in α-glucosidase inhibition by 35% was found for complete hydrolysates but no significant change for the <1 kDa fractions, after the simulated gastrointestinal digestion.…”

mentioning

confidence: 86%

“…The dehulled bean flour was then mixed with water at a ratio 1:10 and pH adjusted to 8.0 with 0. Alcalase and bromelain hydrolysates were further hydrolyzed with pepsin-pancreatin to mimic gastrointestinal digestion following the method described by Oseguera-Toledo et al (2011).…”

Section: Bean Flour and Protein Isolatementioning

confidence: 99%

Hard-to-cook bean ( Phaseolus vulgaris L.) proteins hydrolyzed by alcalase and bromelain produced bioactive peptide fractions that inhibit targets of type-2 diabetes and oxidative stress

Oseguera‐Toledo

Mejía

Amaya-Llano

2015

Food Research International

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Common bean (Phaseolus vulgaris L.) hydrolysates inhibit inflammation in LPS-induced macrophages through suppression of NF-κB pathways

Cited by 88 publications

References 31 publications

Simultaneous release of peptides and phenolics with antioxidant, ACE-inhibitory and anti-inflammatory activities from pinto bean (Phaseolus vulgaris L. var. pinto) proteins by subtilisins

Simultaneous release of peptides and phenolics with antioxidant, ACE-inhibitory and anti-inflammatory activities from pinto bean (Phaseolus vulgaris L. var. pinto) proteins by subtilisins

Germination of Phaseolus vulgaris and alcalase hydrolysis of its proteins produced bioactive peptides capable of improving markers related to type-2 diabetes in vitro

Hard-to-cook bean ( Phaseolus vulgaris L.) proteins hydrolyzed by alcalase and bromelain produced bioactive peptide fractions that inhibit targets of type-2 diabetes and oxidative stress

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