Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH

Cian, Raúl E.; Vioque, Javier; Drago, Silvina Rosa

doi:10.1016/j.foodres.2014.12.036

Cited by 71 publications

(42 citation statements)

References 44 publications

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“…[36] It has been reported that β-turn played a vital role in the antioxidant capacity of peptides and the ratio of β-turn to β-sheet could reflect the antioxidant feature of peptides. [48] In the present study, it was found that IPIQY, IPIQYV, and PYYAK significantly inhibited the oxidation of linoleic acid (Figure 2a). Additionally, IPIQY and PYYAK with the presence of (α)-tocopherol dramatically reduced the formation rate of malondialdehyde (Figure 2a).…”

Section: Interaction Between Milk Oligopeptide and (α)-Tocopherolsupporting

confidence: 52%

Milk oligopeptide inhibition of (α)-tocopherol fortified linoleic acid oxidation

Yuan

Gong

Tang

et al. 2019

International Journal of Food Properties

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This study investigated the effect of milk oligopeptides and (α)-tocopherol on inhibition of linoleic acid oxidation using Fe 2+ -vitamin C induced linoleic acid oxidation model through analysis of malondialdehyde, peroxide value, and conjugated diene and triene in the model. The alteration of milk oligopeptides maximal absorption wavelength, fluorescent feature, and secondary structure were further investigated to elucidate the interactions between milk oligopeptide and (α)-tocopherol that altered the inhibitory effect of linoleic acid oxidation. Results showed that Pro-Tyr-Tyr-Ala-Lys (PYYAK) and Ile-Pro-Ile-Gln-Tyr (IPIQY) with (α)-tocopherol significantly inhibited the oxidation of linoleic acid and reduced the formation of malondialdehyde by 38% and 41%, respectively. Additionally, Ile-Pro-Ile-Gln-Tyr-Val (IPIQYV) and (α)-tocopherol synergistically reduced the peroxide value in the model by 36.8%. Milk oligopeptides exhibited a blue shift on its maximal absorption wavelength, and their absorbance value decreased with the increase of the (α)-tocopherol concentration. The fluorescent intensity of milk oligopeptides was reduced with the addition of (α)-tocopherol and such fluorescent intensity reductions resulted from the static quenching process through the formation of milk oligopeptide-(α)tocopherol complex. Fourier transform infrared spectroscopy analysis revealed that (α)-tocopherol significantly altered the secondary structure of milk oligopeptides and the percentage of β-turn obviously increased in milk oligopeptide-(α)-tocopherol complex. These indicated that the inhibition of linoleic acid oxidation might result from complex formed between milk oligopeptide and (α)-tocopherol through inter-molecular interactions. ARTICLE HISTORY

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Section: Interaction Between Milk Oligopeptide and (α)-Tocopherolsupporting

confidence: 52%

Milk oligopeptide inhibition of (α)-tocopherol fortified linoleic acid oxidation

Yuan

Gong

Tang

et al. 2019

International Journal of Food Properties

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“…The observed increase in antioxidant activity could be attributed to a higher concentration of polyphenols as strong pH variations and pepsin may affect the integrity of cell walls, facilitating the liberation of phenolic and antioxidant compounds not detected in initial phases. In addition, hydrolysis of wheat-and broccoli-derived proteins could result in peptides with antioxidant properties (Cian, Vioque, & Drago, 2015;Niu, Jiang, & Pan, 2013). Also, different pH values can affect racemization of molecules creating two different chiral enantiomers and altering their biological activities, rendering antioxidants more reactive early in the digestive process (Jamali, Bjørnsdottir, Nordfang, & Hansen, 2008…”

Section: Resistance To In Vitro Digestionmentioning

confidence: 99%

Bioaccessibility, physicochemical, sensorial, and nutritional characteristics of bread containing broccoli co-products

Lafarga

Gallagher

Bademunt

et al. 2019

J Food Process Preserv

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The effects of the inclusion of industrial broccoli co‐products namely stalks and leaves into bread on physicochemical and nutritional properties were evaluated. Incorporation of powdered broccoli co‐products at a concentration of 2% (w/w) into bread formulations resulted in decreased weight and specific volumes when compared to the control (p < 0.05). Broccoli‐containing breads showed an increased green hue and a higher crust and crumb color intensity (p < 0.05). Incorporation of broccoli co‐products into bread formulations significantly increased the total phenolic content and antioxidant capacity of the breads (p < 0.05). The overall acceptance and appearance of the breads were not affected by broccoli incorporation. The phenolic content and antioxidant capacity of the three formulations increased after the gastric and intestinal phases of digestion when compared to the initial stage, measured from a methanol:water extract (p < 0.05). Results obtained herein could open novel commercial opportunities for food processors and reduce the amount of food discarded as waste. Practical applications In recent decades, functional foods have gained increased consumer interest and are currently one of the hot trends in the food industry. In addition, sustainable food production and waste valorization are becoming important issues in the food industry, where high amounts of co‐products are generated. A large percentage of the total mass of broccoli plants is discarded as waste or used for low‐value purposes. Broccoli co‐products are rich in bioactive compounds. Therefore, enrichment of bread with bioactive compounds obtained from broccoli co‐products is both an economic and environmentally attractive option for food processors.

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“…7 The bioactive properties of wheat gluten hydrolysates such as their antioxidant and antihypertensive properties have been demonstrated in vitro. [8][9][10] Numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptides have been identified within wheat gliadins and glutenins during in silico studies. 11,12 DPP-IV is a metabolic enzyme which can bring about the degradation and inactivation of incretins (e.g., glucagon like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP)).…”

Section: Introductionmentioning

confidence: 99%

Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties

et al. 2017

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Wheat gluten, a Pro-rich dietary protein, was investigated for its potential to produce dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during enzymatic hydrolysis with Debitrase HYW20. Nine gluten hydrolysates (H1-H9) were generated using a 2 factor × 3 level design of experiments (DOE) including the incubation temperature (40, 50 and 60 °C) and the enzyme: substrate ratio (E : S, 0.5, 1.0 and 1.5% (w/w)). Their DPP-IV half maximal inhibitory concentration (IC) ranged from 0.24 ± 0.02 (H9) to 0.66 ± 0.06 mg mL (H2A and H7) and their degree of hydrolysis (DH) from 31.7 ± 0.9 (H7) to 62.2 ± 3.0% (H6). Gluten and H9, the most potent DPP-IV inhibitory hydrolysate, were subjected to simulated gastrointestinal digestion (SGID), yielding Gluten_CorPP and H9_CorPP, respectively. H9_CorPP had a higher DPP-IV inhibitory potency than Gluten_CorPP (i.e., DPP-IV IC values of 0.33 ± 0.03 vs. 1.45 ± 0.26 mg mL, respectively). H9 and H9_CorPP both contained relatively potent DPP-IV inhibitory peptides such as Val-Pro-Leu, Trp-Leu and Trp-Pro which were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS). In addition, several sequences possessing features of DPP-IV inhibitory peptides, mostly consisting of a penultimate or C-terminal Pro, were identified within H9. The presence of Pro-containing peptides within H9 may contribute to its stability to digestive enzymes. Gluten hydrolysates may have antidiabetic potential for humans.

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Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH

Cited by 71 publications

References 44 publications

Milk oligopeptide inhibition of (α)-tocopherol fortified linoleic acid oxidation

Milk oligopeptide inhibition of (α)-tocopherol fortified linoleic acid oxidation

Bioaccessibility, physicochemical, sensorial, and nutritional characteristics of bread containing broccoli co-products

Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties

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