Correction to: An evaluation of the in vitro antioxidant and antidiabetic potentials of camel and donkey milk peptides released from casein and whey proteins

The increase of knowledge on the composition of donkey milk has revealed marked similarities to human milk, which led to a growing number of investigations focused on testing the potential effects of donkey milk in vitro and in vivo. This paper examines the scientific evidence regarding the beneficial effects of donkey milk on human health. Most clinical studies report a tolerability of donkey milk in 82.6–98.5% of infants with cow milk protein allergies. The average protein content of donkey milk is about 18 g/L. Caseins, which are main allergenic components of milk, are less represented compared to cow milk (56% of the total protein in donkey vs. 80% in cow milk). Donkey milk is well accepted by children due to its high concentration of lactose (about 60 g/L). Immunomodulatory properties have been reported in one study in humans and in several animal models. Donkey milk also seems to modulate the intestinal microbiota, enhance antioxidant defense mechanisms and detoxifying enzymes activities, reduce hyperglycemia and normalize dyslipidemia. Donkey milk has lower calorie and fat content compared with other milks used in human nutrition (fat ranges from 0.20% to 1.7%) and a more favourable fatty acid profile, being low in saturated fatty acids (3.02 g/L) and high in alpha-linolenic acid (about 7.25 g/100 g of fat). Until now, the beneficial properties of donkey milk have been mostly related to whey proteins, among which β-lactoglobulin is the most represented (6.06 g/L), followed by α-lactalbumin (about 2 g/L) and lysozyme (1.07 g/L). So far, the health functionality of donkey milk has been tested almost exclusively on animal models. Furthermore, in vitro studies have described inhibitory action against bacteria, viruses, and fungi. From the literature review emerges the need for new randomized clinical trials on humans to provide stronger evidence of the potential beneficial health effects of donkey milk, which could lead to new applications as an adjuvant in the treatment of cardiometabolic diseases, malnutrition, and aging.

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Binding of Gallic Acid and Epigallocatechin Gallate to Heat-Unfolded Whey Proteins at Neutral pH Alters Radical Scavenging Activity of in Vitro Protein Digests

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.7b03006 ◽

2017 ◽

Vol 65 (38) ◽

pp. 8443-8450 ◽

Cited By ~ 14

Author(s):

Yanyun Cao ◽

Youling L. Xiong

Keyword(s):

Gallic Acid ◽

Radical Scavenging Activity ◽

Whey Proteins ◽

Radical Scavenging ◽

Epigallocatechin Gallate ◽

Scavenging Activity ◽

Neutral Ph ◽

Protein Digests ◽

Vitro Protein

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Scientific Background of Dairy Protein Digestibility: A Review

Journal of Food Science and Technology Nepal ◽

10.3126/jfstn.v7i0.10560 ◽

2014 ◽

Vol 7 ◽

pp. 1-8 ◽

Cited By ~ 2

Author(s):

Ashok Kumar Shrestha

Keyword(s):

Amino Acids ◽

Whey Proteins ◽

Protein Digestibility ◽

In Vitro Digestion ◽

Dairy Proteins ◽

Dairy Foods ◽

Dairy Protein ◽

Protein Rich ◽

And Control

Recent advances have shown that differences in compositional, structural and physical properties of caseins and whey proteins affect their digestion and absorption behavior, hormonal response, satiety effect and other physiological effects. For example, the ingestion of whey protein cause fast, high and transient increase of amino acids ‘fast protein’, whereas casein induce slower, lower and prolonged increase of ‘slow protein’ in the gut. Knowledge of, and control over, the rate and nature of digestive breakdown of dairy proteins provides a potential basis for product/process innovation through identifying ingredients and formulations that provide desired nutrient delivery profiles. With this background, the aim of our current review paper is to understand the digestion behavior of various protein-rich milk powders and their potential use in formulation of dairy foods for controlled release of amino acids and energy. Currently available in vitro protein digestibility methods to measure or predict the dairy protein digestibility were also investigated. The author has also presented the preliminary results of ongoing study on in vitro digestion of various commercial proteins powders.DOI: http://dx.doi.org/10.3126/jfstn.v7i0.10560 J. Food Sci. Technol. Nepal, Vol. 7 (1-8), 2012

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Are Faba Bean and Pea Proteins Potential Whey Protein Substitutes in Infant Formulas? An In Vitro Dynamic Digestion Approach

Foods ◽

10.3390/foods9030362 ◽

2020 ◽

Vol 9 (3) ◽

pp. 362

Author(s):

Linda Le Roux ◽

Olivia Ménard ◽

Raphaël Chacon ◽

Didier Dupont ◽

Romain Jeantet ◽

...

Keyword(s):

Faba Bean ◽

Whey Proteins ◽

Milk Proteins ◽

Protein Digestibility ◽

Cow Milk ◽

Partial Substitution ◽

Infant Formulas ◽

Pea Proteins

Infant formulas (IFs) are used as substitutes for human milk and are mostly based on cow milk proteins. For sustainability reasons, animal protein alternatives in food are increasingly being considered, as plant proteins offer interesting nutritional and functional benefits for the development of innovative IFs. This study aimed to assess how a partial substitution (50%) of dairy proteins with faba bean and pea proteins influenced the digestibility of IFs under simulated dynamic in vitro digestion, which were set up to mimic infant digestion. Pea- and faba bean-based IFs (PIF and FIF, respectively) have led to a faster aggregation than the reference milk-based IF (RIF) in the gastric compartment; that did not affect the digesta microstructure at the end of digestion. The extent of proteolysis was estimated via the hydrolysis degree, which was the highest for FIF (73%) and the lowest for RIF (50%). Finally, it was apparent that in vitro protein digestibility and protein digestibility-corrected amino acid score (PDCAAS)-like scores were similar for RIF and FIF (90% digestibility; 75% PDCAAS), but lower for PIF (75%; 67%). Therefore, this study confirms that faba bean proteins could be a good candidate for partial substitution of whey proteins in IFs from a nutritional point of view, provided that these in vitro results are confirmed in vivo.

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Interactions between whey proteins and cranberry juice after thermal or non-thermal processing during in vitro gastrointestinal digestion

Food & Function ◽

10.1039/d0fo00177e ◽

2020 ◽

Vol 11 (9) ◽

pp. 7661-7680

Author(s):

Karen A. Rios-Villa ◽

Mrittika Bhattacharya ◽

Ellia H. La ◽

Daniela Barile ◽

Gail M. Bornhorst

Keyword(s):

Whey Protein ◽

Thermal Processing ◽

Whey Proteins ◽

Protein Digestibility ◽

Cranberry Juice ◽

Gastrointestinal Digestion ◽

In Vitro Gastrointestinal Digestion

This study entails the possible interactions between whey protein and cranberry juice after processing, impacting either the protein digestibility or the bioaccessibility of cranberry antioxidants using an in vitro gastrointestinal digestion model.

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Stability and in vitro digestibility of emulsions containing lecithin and whey proteins

Food & Function ◽

10.1039/c3fo60156k ◽

2013 ◽

Vol 4 (9) ◽

pp. 1322 ◽

Cited By ~ 37

Author(s):

Raphaela Araujo Mantovani ◽

Ângelo Luiz Fazani Cavallieri ◽

Flavia Maria Netto ◽

Rosiane Lopes Cunha

Keyword(s):

Whey Proteins ◽

In Vitro Digestibility

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Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species

Journal of Dairy Research ◽

10.1017/s0022029900027345 ◽

1993 ◽

Vol 60 (1) ◽

pp. 55-63 ◽

Cited By ~ 30

Author(s):

M. Dolores Pérez ◽

Pilar Puyol ◽

José Manuel Ena ◽

Miguel Calvo

Keyword(s):

Fatty Acids ◽

Guinea Pig ◽

Serum Albumin ◽

Whey Protein ◽

Whey Proteins ◽

Gel Filtration ◽

Ruminant Species ◽

Β Lactoglobulin

SummaryThe interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolated from milk, had ˜ 0·5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained ˜ 4·5, 2·9 and 4·7 mol fatty acids/mol protein respectively. However, β-lactoglobulin from horse and pig milk had neither fatty acids physiologically bound nor the ability to bind them in vitro. Albumin was the only whey protein detected with bound fatty acids in these species as well as in human and guinea pig. This suggests that the ability of ruminant β-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.

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Antibacterial peptides derived from caprine whey proteins, by digestion with human gastrointestinal juice

British Journal Of Nutrition ◽

10.1017/s0007114511001085 ◽

2011 ◽

Vol 106 (6) ◽

pp. 896-905 ◽

Cited By ~ 38

Author(s):

Hilde Almaas ◽

Ellen Eriksen ◽

Camilla Sekse ◽

Irene Comi ◽

Ragnar Flengsrud ◽

...

Keyword(s):

Antibacterial Effect ◽

Consensus Sequence ◽

Whey Proteins ◽

Lactobacillus Rhamnosus ◽

Proteolytic Processing ◽

Duodenal Juice ◽

Multiple Sequence ◽

Strong Activity ◽

Gastrointestinal Enzymes

Peptides in caprine whey were identified afterin vitrodigestion with human gastrointestinal enzymes in order to determine their antibacterial effect. The digestion was performed in two continuing steps using human gastric juice (pH 2·5) and human duodenal juice (pH 8) at 37°C. After digestion the hydrolysate was fractionated and 106 peptides were identified. From these results, twenty-two peptides, located in the protein molecules, were synthesised and antibacterial activity examined. Strong activity of the hydrolysates was detected againstEscherichia coliK12,Bacillus cereusRT INF01 andListeria monocytogenes, less activity againstStaphylococcus aureusATCC 25 923 and no effect onLactobacillus rhamnosusGG. The pure peptides showed less antibacterial effect than the hydrolysates. When comparing the peptide sequences from human gastrointestinal enzymes with previously identified peptides from non-human enzymes, only two peptides, β-lactoglobulin f(92–100) and β-casein f(191–205) matched. No peptides corresponded to the antibacterial caprine lactoferricin f(14–42) or lactoferrampin C f(268–284). Human gastrointestinal enzymes seem to be more complex and have different cleavage points in their protein chains compared with purified non-human enzymes. Multiple sequence alignment of nineteen peptides showed proline-rich sequences, neighbouring leucines, resulting in a consensus sequence LTPVPELK. In such a way proline and leucine may restrict further proteolytic processing. The present study showed that human gastrointestinal enzymes generated different peptides from caprine whey compared with non-human enzymes and a stronger antibacterial effect of the hydrolysates than the pure peptides was shown. Antimicrobial activity against pathogens but not against probiotics indicate a possible host-protective activity of whey.

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