News & Research

Whey protein boosts the antioxidant profile by enhancing the activities of crucial antioxidant enzymes in a tissue-specific manner.

Whey protein, a by-product of cheese industry, is harmful for the environment (i.e., surface and subterranean waters, soil) and, therefore, for humans due to its high polluting burden. Concomitantly, it has been reported that it is a mixture with potent antioxidant action since it is rich in cysteine residues, which are necessary for glutathione synthesis in vivo. On this basis, this study intended to examine the role of whey protein on the intensification of tissue antioxidant arsenal.
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Anti-inflammatory effects of a special carbohydrate-whey protein cake after exhaustive cycling in humans.

Intense exercise induces increased levels of pro-inflammatory and anti-inflammatory cytokines. Thus, the purpose of this study was to examine the effects of a special cake (consisting of carbohydrate to whey protein 3.5:1) vs. an isocaloric carbohydrate cake on inflammatory markers after exhaustive cycling in humans. Nine subjects received either the experimental or placebo cake in a counterbalanced fashion using a crossover, double-blind, repeated-measures design.
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Increase in antioxidant activity by sheep/goat whey protein through nuclear factor-like 2 (Nrf2) is cell type dependent.

The aim of the present study was to investigate the molecular mechanisms through which sheep/goat whey protein exerts its antioxidant activity. Thus, it was examined whey protein’s effects on the expression of transcription factor, nuclear factor-like 2 (Nrf2) and on the expression and activity of a number of antioxidant and phase II enzymes, superoxide dismutase (SOD), catalase (CAT), heme oxygenase 1 (HO-1), synthase glutamyl cysteine (GCS) and glutathione-s-transferase (GST), in muscle C2C12 and EA.hy926 endothelial cells.
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Antioxidant effects of whey protein on muscle C2C12 cells.

In the present study, the in vitro scavenging activity of sheep whey protein against free radicals, as well as its reducing power were determined and compared with that of beef protein, soy protein and cow whey protein. Moreover, the possible protective effects of sheep whey protein from tert-butyl hydroperoxide (tBHP)-induced oxidative stress in muscle C2C12 cells were determined by assessing oxidative stress markers by flow cytometry and spectrophotometry.
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The Strong Antioxidant Sheep/Goat Whey Protein Protects Against mTOR Overactivation: A Mode of Action Mimicking Fasting.

Whey protein, a by-product of the cheese industry, can be putatively used as a functional food due to its beneficial health properties. The main objective of the present study was to assess in vivo the effect of a sheep/goat whey protein on the plasma amino acid profile and mammalian target of rapamycin (mTOR), a regulator of skeletal myogenesis. A control group was fed with a standard commercial diet while the experimental group received a standard commercial diet plus sheep/goat whey protein for 28 days.
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Antioxidant Effects of Sheep Whey Protein on Endothelial Cells.

Excessive production of reactive oxygen species (ROS) may cause endothelial dysfunction and consequently vascular disease. In the present study, the possible protective effects of sheep whey protein (SWP) from tert-butyl hydroperoxide- (tBHP-) induced oxidative stress in endothelial cells (EA.hy926) were assessed using oxidative stress biomarkers. These oxidative stress biomarkers were glutathione (GSH) and ROS levels determined by flow cytometry.
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Effects of sheep/goat whey protein dietary supplementation on the redox status.

The purpose of the present study is to estimate the effects of sheep/goat whey protein dietary supplementation on the redox status of blood and tissues of α control group.
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Glycemic response of a carbohydrate-protein bar with ewe-goat whey.

In this study we examined the glycaemic index (GI) and glycaemic load (GL) of a functional food product, which contains ewe-goat whey protein and carbohydrates in a 1:1 ratio. Nine healthy volunteers, (age, 23.3 ± 3.9 years; body mass index, 24.2 ± 4.1 kg·m2; body fat %, 18.6 ± 10.0) randomly consumed either a reference food or amount of the test food both with equal carbohydrate content in two visits. In each visit, seven blood samples were collected; the first sample after an overnight fast and the remaining six at 15, 30, 45, 60, 90 and 120 min after the beginning of food consumption.
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