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

Polanco-Lugo, Erik; Dávila-Ortíz, Gloria; Betancur‐Ancona, David; Chel‐Guerrero, Luis

doi:10.1590/1678-457x.6349

Cited by 44 publications

(22 citation statements)

References 41 publications

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“…It has been observed that hydrolysates have the ability to decrease reactivity of free radicals (Elias et al, 2008). The TEAC value of treatment 8 in mM/mg protein was of 100.76, this value was higher than the reported by Torruco-Uco et al (2009) Polanco-lugo et al (2014) reported the TEAC in extensive hydrolysate of P. lunatus with a value of 13.2 mM/mg protein, and this value was lowest in comparison to the obtained in this study. Amino acids like Tyr, Met, Trp, leu, His and lys were widely reported as having high antioxidant activity (Chen et al, 1998).…”

Section: Protein Releasedcontrasting

confidence: 76%

“…The value in the intestinal system of all treatments was better in comparison to the non-encapsulated fraction (0.37 mg/ml of IC 50 ). Polanco-lugo et al (2014) reported values for ACE inhibition for extensive hydrolysates from P. lunatus with a value of 0.321 mg/ml of IC 50. The values of treatments in IS were better gums CFG:SA could be use in the encapsulation of cells or protein (not fractions) encapsulation but implementing another encapsulation technique, as mentioned by Yeo et al (2001).…”

Section: Ace-i and Antioxidant Activitymentioning

confidence: 99%

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Evaluation of some residual bioactivities of microencapsulated Phaseolus lunatus protein fraction with carboxymethylated flamboyant (Delonix regia) gum/sodium alginate

Sandovai-Peraza¹,

Betancur‐Ancona²,

Gallegos-Tintoré³

et al. 2014

Food Sci. Technol (Campinas)

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Recent studies have shown the beneficial effect of peptides, an unexploited source could be Phaseolus lunatus being an important raw material for those functional products in order to improve their utilization. In addition to improve the beneficial effect of bioactive peptides the microencapsulation could be a way to protect the peptides against the environment to which they are exposed. P. lunatus protein fraction (<10 kDa of weight) was encapsulated using a blend of carboxymethylated flamboyant gum (CFG) and sodium alginate (SA) at different concentrations of CaCl 2 and hardening times. After in vitro digestion of microcapsules the residual activity, in the intestinal system, both inhibition of agiotensin-converting enzyme (I-ACE) and antioxidant activity obtained were in a range of 0.019-0.136 mg/ml and 570.64-813.54 mM of TEAC respectively. The microencapsulation employed CFG/SA blends could be used controlled delivery of peptide fractions with potential use as a nutraceutical or therapeutic agents.

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Section: Protein Releasedcontrasting

confidence: 76%

Section: Ace-i and Antioxidant Activitymentioning

confidence: 99%

Evaluation of some residual bioactivities of microencapsulated Phaseolus lunatus protein fraction with carboxymethylated flamboyant (Delonix regia) gum/sodium alginate

Sandovai-Peraza¹,

Betancur‐Ancona²,

Gallegos-Tintoré³

et al. 2014

Food Sci. Technol (Campinas)

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“…All 20 amino acids found in proteins have the potential to interact with free radicals; however, the most reactive amino acids tend to be those containing either nucleophilic sulfur-containing side chains (cysteine and methionine) or aromatic side chains (tryptophan, tyrosine and phenylalanine) (Elias et al, 2008). For Polanco-Lugo et al (2014), the high exposure of hydrophobic amino acids residues in Phaseolus lunatus protein hydrolysate may have an impact on antioxidant activity. Stanojevic et al, (2012) reported that the main protein found in okara is glycinin (11S protein), whose peptides contain cysteine and methionine residues (Murphy, 2008).…”

Section: Antioxidant Activitymentioning

confidence: 99%

“…The differences in the antioxidant activities of the hydrolysates with similar DH could be due to different catalytic actions and enzyme specificity, which can affect the number and location of the peptide linkages hydrolyzed. Thus, there is a release of different peptides in terms of size, level and amino acid composition (Polanco-Lugo et al, 2014). Alcalase is an endopeptidase that cleaves a protein bond located on the inside of the molecule, releasing two peptides of relatively substantial molecular weight.…”

Section: Antioxidant Activitymentioning

confidence: 99%

“…Therefore, enzymatic hydrolysis favors the exposure of antioxidant amino acids in proteins, increasing antioxidant activity of peptides. Several factors affect the antioxidant properties of protein hydrolysates, and depend on: type of protein and enzyme, degree of hydrolysis and pretreatment of the substrate (Elias et al, 2008;Pazinatto et al, 2013;Polanco-Lugo et al, 2014). This activity occurs by specific mechanisms including the capacity of amino acid residues to donate electrons to free radicals.…”

Section: Introductionmentioning

confidence: 99%

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Influence of the degree of hydrolysis and type of enzyme on antioxidant activity of okara protein hydrolysates

et al. 2016

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The objective of this work was to evaluate the antioxidant activity of protein hydrolysates obtained by the enzymatic hydrolysis of okara using an endopeptidase (Alcalase) and exopeptidase (Flavourzyme). The reaction was monitored by the pH-stat procedure in which five aliquots were collected during the hydrolysis by each enzyme, corresponding to different degrees of hydrolysis (DH). The antioxidant activities of the aliquots were evaluated by the ABTS, DPPH and FRAP methods. For the hydrolysates obtained using Alcalase, the antioxidant activities increased from: 68.6 to 99.5% (ABTS), 14.5 to 17.7% (DPPH) and 222.6 to 684.9 µM Trolox (FRAP), when the DH varied from 0 to 33.6%. With respect to Flavourzyme, the results were: 67.2 to 88.2% (ABTS), 9.5 to 18.5% (DPPH) and 168.0 to 360.3 µM Trolox (FRAP), when the DH increased up to 5.8%. The results showed that the protein hydrolysates had antioxidant capacities, which were influenced by the degree of hydrolysis and the type of enzyme.

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Physicochemical properties of enzymatically modified pea protein‐enriched flour treated by different enzymes to varying levels of hydrolysis

et al. 2019

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Background and objectives Air‐classified pea protein‐enriched flour (PPEF) was modified with trypsin, Savinase, papain, and pepsin to achieve 2%–4% and 10%–12% degrees of hydrolysis, and the surface and functional properties of the hydrolyzed products were assessed. Findings Surface hydrophobicity increased from 13.3 to 48.5 A.U. with papain treatment. Surface charge became more electronegative from −12.6 to −19.0 mV with pepsin treatment. However, solubility of hydrolyzed PPEF at all pH values tested (4.0, 7.0, and 10.0), regardless of enzyme treatment, decreased. Low solubility of hydrolyzed proteins negatively impacted solubility‐dependant functional properties: foaming properties and emulsifying properties decreased. However solubility‐independent properties (water‐ and oil‐holding capacity; WHC and OHC, respectively) improved with proteolysis, increasing from 0.6 g/g to 1.4–2.0 g/g and from 0.7 g/g to 1.0–1.5 g/g, respectively. Conclusions Papain treatment yielded the best results in terms of both OHC and WHC of PPEF. Significance and novelty The resultant hydrolyzates have potential for baked goods and processed meat applications because of their increased OHC and WHC.

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

Cited by 44 publications

References 41 publications

Evaluation of some residual bioactivities of microencapsulated Phaseolus lunatus protein fraction with carboxymethylated flamboyant (Delonix regia) gum/sodium alginate

Evaluation of some residual bioactivities of microencapsulated Phaseolus lunatus protein fraction with carboxymethylated flamboyant (Delonix regia) gum/sodium alginate

Influence of the degree of hydrolysis and type of enzyme on antioxidant activity of okara protein hydrolysates

Physicochemical properties of enzymatically modified pea protein‐enriched flour treated by different enzymes to varying levels of hydrolysis

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