Pigeon pea enzymatic protein hydrolysates and ultrafiltration peptide fractions as potential sources of antioxidant peptides: An in vitro study

Olagunju, Aderonke Ibidunni; Omoba, Olufunmilayo Sade; Enujiugha, Victor N.; Alashi, Adeola M.; Aluko, Rotimi E.

doi:10.1016/j.lwt.2018.07.003

Cited by 83 publications

(82 citation statements)

References 44 publications

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“…The ABTS radical-scavenging activity of the control (collagen suspension), CH-Alcalase, and CH-Alcalase < 3 kDa at different concentrations is shown (Figure 5A). ABTS radical scavenging activity of peptides assay is important to exclusively measure the ability of an antioxidant peptide to induce a hydrogen atom transfer [25]. ABTS radical-scavenging effects of all treatments increased in a concentration-dependent manner ( p < 0.05).…”

Section: Resultsmentioning

confidence: 99%

Anti-Oxidative and Anti-Aging Activities of Porcine By-Product Collagen Hydrolysates Produced by Commercial Proteases: Effect of Hydrolysis and Ultrafiltration

Hong

Min

2019

Molecules

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To investigate methods for improving the processing of porcine waste, porcine skin was hydrolyzed using different commercially available proteases (Alcalase, Flavorzyme, Neutrase, Bromeline, Protamex, and Papain) under several optimal conditions. Following enzymatic hydrolysis, the collagen hydrolysates (CHs) were fractionated by molecular weight (3 kDa) via membrane ultrafiltration. The CHs were analyzed for physical properties (pH, protein recovery, free amino group content, molecular weight distribution, and amino composition) as well as for functional properties (antioxidant activities and anti-aging activities). Among the CHs, CHs hydrolyzed by Alcalase (CH-Alcalase) exhibited the highest degree of hydrolysis compared to other CHs. Both “CH-Alcalase” and “CH-Alcalase < 3 kDa” fractions showed a considerably high antioxidant activity and collagenase inhibition activity. Therefore, resulting bioactives have potential for development as antioxidants and anti-aging ingredients in the food, cosmetics, and pharmaceuticals, from animal by-products.

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Section: Resultsmentioning

confidence: 99%

Anti-Oxidative and Anti-Aging Activities of Porcine By-Product Collagen Hydrolysates Produced by Commercial Proteases: Effect of Hydrolysis and Ultrafiltration

Hong

Min

2019

Molecules

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“…According to Olagunju et al [25] and Ren et al [26], enrichment of bioactive peptide from protein hydrolysates could be carried out using ultrafiltration method, which was employed and modified as ultrafiltration-centrifugation technique in present study. The digested peptide was fractionated into three groups according to molecular weight, i.e., 100-500, 500-1000, and 1000-3000 Da.…”

Section: Resultsmentioning

confidence: 99%

Optimization and Identification of Antioxidant Peptide from Underutilized Dunaliella salina Protein: Extraction, In Vitro Gastrointestinal Digestion, and Fractionation

Xia

Zhai

Huang

et al. 2019

BioMed Research International

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DPPH• scavenging peptides (<3kDa) from underutilized Dunaliella salina protein were obtained by the following successive treatment, i.e., ultrasound extraction, simulated in vitro gastrointestinal digestion hydrolyzation, and membrane ultrafiltration classification. The optimal condition for ultrasound-assisted extraction was an ultrasound wave with 800 W of power treating a mixture of 60 mL of 1.0 mol L−1 NaOH and 2 g algae powder for 15 min. A high correlation (r=0.8146) between DPPH• scavenging activity and yield of the intact peptides showed their antioxidant capacity. Simulated in vitro digestion assay resulted in excellent DPPH• scavenging activity of the total peptide, amounting to (86.5 ± 10.1)%, comparing with the nondigestion samples at (46.8 ± 6.5)%. After fractionation, the 500-1000 Da fraction exhibited the highest DPPH• scavenging activity (81.2 ± 4.0)%, increasing 1.5 times due to digestion. Then, the 500-1000 Da fraction was analyzed by RPLC-Q Exactive HF mass spectrometer, and 4 novel peptides, i.e., Ile-Leu-Thr-Lys-Ala-Ala-Ile-Glu-Gly-Lys, Ile-Ile-Tyr-Phe-Gln-Gly-Lys, Asn-Asp-Pro-Ser-Thr-Val-Lys, and Thr-Val-Arg-Pro-Pro-Gln-Arg, were identified. From these amino acid sequences, hydrophobic residues accounted for 56%, which indicated their high antioxidant property. The results indicated that underutilized protein of Dunaliella salina could be a potential source of antioxidative peptides through simulated in vitro gastrointestinal digestion.

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“…A major challenge of the in silico approach is the dearth of in vitro analysis to confirm bioactivity (Agyei et al, ). Using the classic approach, recent studies reported that fermented/hydrolyzed pigeon pea seeds/flour have strong potential for exploration as antioxidative and antihypertensive food ingredients (Nawaz et al, ; Olagunju, Omoba, Enujingha, Alashi, & Aluko, ; Olagunju, Omoba, Enujingha, Alashi, & Aluko, ; Olagunju et al, ). The objectives for this study were to use the bioinformatics approach to assess the potential of nutrient reservoir (storage) proteins in pigeon pea as precursors of DPP‐4‐inhibiting peptides, and to evaluate the relationship between structural features of the proteins and biofunctional parameters of released peptides.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

Boachie

Okoro²,

Imai

et al. 2019

J Food Biochem

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Abbreviations: ANS, 8-anilino-1-naphthalenesulphonic acid; BSA, bovine serum albumin; DPP-4, dipeptidyl peptidase-4; GIP, glucose-dependent insulinotropic polypeptide; GLP-1, glucagon-like peptide-1; GRAVY, grand average of hydropathicity; OPA, o-phthalaldehyde; pI, theoretical isoelectric point; RMSE, root mean square error; T2DM, type 2 diabetes mellitus; UPLC, ultra-performance liquid chromatography. AbstractIn silico and in vitro parameters were used to assess the potential of pigeon pea (Cajanus cajan) nutrient reservoir proteins as sources of dipeptidyl peptidase (DPP)-4 inhibitors. In silico, 40 pigeon pea proteins evaluated had 46% of amino acids associated with DPP-4 inhibition. After virtual hydrolysis, pepsin had the highest frequency of release and bioactivity of released DPP-4 inhibiting peptides, compared to papain and thermolysin. In vitro, thermolysin released the most active DPP-4 inhibitors.The protein hydrolysates contained similar amino acids but different particle sizes.Thus, the bioactivity patterns are attributable to the different nature and behavior of proteins/peptides under actual and virtual conditions. Using eight physicochemical variables, a random forest model with moderate prediction accuracy was developed for predicting DPP-4 inhibitory activity of papain hydrolysates. The findings demonstrate that proteins from pigeon pea are precursors of DPP-4 inhibitors, with potential use in formulating functional food for managing type 2 diabetes. | In silico analysis of physicochemical properties of pigeon pea proteinsPhysicochemical properties of the 40 mature pigeon pea proteins/ domains and BSA were calculated using the ProtParam feature of UniProtKB. The properties include the protein chain length, theoretical isoelectric point (pI), molecular weight, grand average of K E Y W O R D S bioactive peptides, bioinformatics, Cajanus cajan, dipeptidyl peptidase-4, in silico, pigeon pea S U PP O RTI N G I N FO R M ATI O N Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Boachie RT, Okoro FL, Imai K, et al. Enzymatic release of dipeptidyl peptidase-4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments. J Food Biochem.

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Pigeon pea enzymatic protein hydrolysates and ultrafiltration peptide fractions as potential sources of antioxidant peptides: An in vitro study

Cited by 83 publications

References 44 publications

Anti-Oxidative and Anti-Aging Activities of Porcine By-Product Collagen Hydrolysates Produced by Commercial Proteases: Effect of Hydrolysis and Ultrafiltration

Anti-Oxidative and Anti-Aging Activities of Porcine By-Product Collagen Hydrolysates Produced by Commercial Proteases: Effect of Hydrolysis and Ultrafiltration

Optimization and Identification of Antioxidant Peptide from Underutilized Dunaliella salina Protein: Extraction, In Vitro Gastrointestinal Digestion, and Fractionation

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

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