Antioxidant mechanism of potato protein hydrolysates against in vitro oxidation of reduced glutathione

Udenigwe, Chibuike C.; Udechukwu, M. Chinonye; Yiridoe, Conrad; Gibson, Angus; Gong, Min

doi:10.1016/j.jff.2015.11.004

Cited by 66 publications

(57 citation statements)

References 25 publications

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“…This is the first evidence of the protective effect of food peptides in oxidized plasma matrix in vitro. We had reported a similar protective effect of peptides using glutathione as the biological target (Udenigwe, Udechukwu, Yiridoe, Gibson, & Gong, ). If bioavailable, it is expected that the spent hen protein‐derived peptides will serve as active molecules in reducing the damaging effects of free radicals and reactive oxygen species.…”

Section: Resultsmentioning

confidence: 70%

Antihypertensive and bovine plasma oxidation-inhibitory activities of spent hen meat protein hydrolysates

et al. 2017

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Hydrolysis of spent hen meat proteins with pepsin and pepsin 1 pancreatin yielded SPH-P and SPH-PPc hydrolysates, respectively. The hydrolysates dose-dependently inhibited activities of human recombinant renin (IC 50 0.34 and 0.52 mg/mL, respectively) and angiotensin I-converting enzyme (ACE, IC 50 0.64 and 0.42 mg/mL, respectively). The hydrolysates had lower cysteine and tryptophan contents but similar contents of other amino acids when compared with the parent spent hen protein isolate. SPH-P, but not SPH-PPc, dose-dependently increased the sulfhydryl content and ferric reducing antioxidant capacity of bovine plasma oxidized with H 2 O 2 , which dem-

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Section: Resultsmentioning

confidence: 70%

Antihypertensive and bovine plasma oxidation-inhibitory activities of spent hen meat protein hydrolysates

et al. 2017

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“…Aqueous suspension of the pigeon pea protein powder (5%, w/v) was hydrolyzed with Pep (pH 2, 37°C), Pap (pH 6, 65°C), and The (pH 8, 50°C) for 4 hr at a 1:100 (w/w) enzyme–substrate ratio (Udenigwe, Udechukwu, Yiridoe, Gibson, & Gong, ). Thereafter, the hydrolysates were adjusted to pH 4 using 3 M HCl to precipitate undigested proteins and then centrifuged at 7,000 g for 30 min at 4°C.…”

Section: Methodsmentioning

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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“…In LA and FA processing, which have slower proteolysis rates, an initial increase in S o was observed, followed by a dip and saturation (Figure c). Contrastingly, with exogenous FL hydrolysis, a negative relationship was observed between DH and S o (Udenigwe et al, ). For FL, S o steadily declined with an increase in DH (ρ = −1.000, p = .0833, n = 4).…”

Section: Resultsmentioning

confidence: 98%

“…Sacrificial antioxidant activity of peptides was assessed based on their ability to protect glutathione (GSH, responsible for the maintenance of redox status in most forms of life) from oxidation due to Fenton's reaction. Udenigwe et al suggested that smaller sized peptides possess better ability to protect GSH via improved solvent and free‐radical accessibility (Udenigwe et al, ). However, it was observed in this study that the salmon visceral hydrolysates with higher DH (Figure c) had a lower capacity to protect GSH (Figure c).…”

Section: Resultsmentioning

confidence: 99%

“…The sacrificial antioxidant capacity of the hydrolysates was assessed using a GSH protection assay modified from Udenigwe, Udechukwu, Yiridoe, Gibson, and Gong (). GSH (80 µg/mL, 300 µL, Sigma‐Aldrich, ON, Canada) was equilibrated with 125 µL of sample hydrolysates (4 mg/mL) for 15 min at RT followed by the addition of 50 µL of FeCl 2 (1 mM) and 25 µL of H 2 O 2 (20 µM).…”

Section: Methodsmentioning

confidence: 99%

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Yield, physicochemical, and antioxidant properties of Atlantic salmon visceral hydrolysate: Comparison of lactic acid bacterial fermentation with Flavourzyme proteolysis and formic acid treatment

Rajendran

Mohan

Khiari

et al. 2018

J Food Process Preserv

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This study compares a cost‐effective microbial method, involving lactic acid (LA) fermentation, with the conventional formic acid (FA) treatment and Flavourzyme (FL) enzymatic hydrolysis for valorizing Atlantic salmon processing waste (Viscera). LA and FA processing approaches relied on production (LA) or addition (FA) of organic acids to lower the pH and activate the inherent proteases in these tissues, whereas FL processing was carried out at the optimum conditions for Flavourzyme (37 °C, pH 7.0). Highest protein hydrolysate fraction recovery (∼57%) was seen in LA fermentation, while FA processing resulted in the highest protein levels (∼87%) in the recovered hydrolysate fraction and lowest residual fraction (∼4%). In general, FL processing demonstrated higher Fe(II) chelation (73%) and ferric reducing capacity (27 mM glutathione equivalent) whereas LA‐hydrolysates showed enhanced sacrificial antioxidant properties. Findings from this study would have implications on the application and production of salmon‐based protein hydrolysates, especially, from the perspective of their functionality. Practical applications Peptides derived from natural sources such as fish products have been extensively reported to exert antioxidant activity that mitigates oxidative stress and providing beneficial effects to human health as well as food storage. Several sources of proteins are being explored for the production of biologically active peptides. Utilizing by‐product streams such as fish processing waste is especially attractive as these are cheaper and rich sources of protein. Therefore, utilizing marine bioprocessing waste for the production food‐grade protein hydrolysates is promising, especially in Atlantic Canada.

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Antioxidant mechanism of potato protein hydrolysates against in vitro oxidation of reduced glutathione

Cited by 66 publications

References 25 publications

Antihypertensive and bovine plasma oxidation-inhibitory activities of spent hen meat protein hydrolysates

Antihypertensive and bovine plasma oxidation-inhibitory activities of spent hen meat protein hydrolysates

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

Yield, physicochemical, and antioxidant properties of Atlantic salmon visceral hydrolysate: Comparison of lactic acid bacterial fermentation with Flavourzyme proteolysis and formic acid treatment

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