Modification of protein structures by altering the whey protein profile and heat treatment affects<i>in vitro</i>static digestion of model infant milk formulas

Halabi, Amira; Croguennec, Thomas; Bouhallab, Saı̈d; Dupont, Didier; Deglaire, Amélie

doi:10.1039/d0fo01362e

Cited by 54 publications

(28 citation statements)

References 65 publications

(76 reference statements)

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“…At the end of the in-vitro gastric processing, the residual intact protein matter (normalised to t = 0 min) accounted for 10.1, 24.0, and 27.0% in the case of total caseins, β-lactoglobulin and α-lactalbumin, respectively. These values are generally in accordance with previous studies, confirming that caseins are more susceptible to pepsinolysis than whey proteins ( Halabi et al, 2020 , Phosanam et al, 2021 ). Even though native whey proteins are generally recognised for their substantially higher intragastric peptic resistance ( Borreani et al, 2016 ), the implementation of thermal processing is known as impacting proportionally to its severity the pepsinolytic breakdown of whey proteins ( Barbé et al, 2014 , Macierzanka et al, 2012 , Peram et al, 2013 ).…”

Section: Resultssupporting

confidence: 92%

“…The hydrolysis progress of the milk proteins was monitored by quantifying the amount of primary amino groups present in the collected food matrix, and gastric and small intestine chymes using the O-phthaldialdehyde (OPA) method of Halabi, Croguennec, Bouhallab, Dupont, and Deglaire (2020) . The food matrix was diluted 50-fold, whilst the gastric and small intestine phases were diluted 25 times.…”

Section: Methodsmentioning

confidence: 99%

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Impact of alfalfa (Medicago sativa L.) galactomannan on the microstructural and physicochemical changes of milk proteins under static in-vitro digestion conditions

2022

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Section: Resultssupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

Impact of alfalfa (Medicago sativa L.) galactomannan on the microstructural and physicochemical changes of milk proteins under static in-vitro digestion conditions

2022

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“…Generally, heat-induced denaturation caused by intense thermal processing promotes digestion of milk proteins [ 186 , 201 , 202 ]. For instance, digestion of caseins in infant formulas heated at 80 °C was faster than the digestion of the unheated counterpart, which could be explained by their smaller micelles covered by denatured whey protein aggregates, thus increasing the accessibility to proteases [ 203 ]. Further, another study showed that upon more intense temperatures of 120 °C, caseins were even more rapidly digested than after pasteurisation at 82 °C [ 204 ].…”

Section: Cow’s Milk-based Infant Formulasmentioning

confidence: 99%

Alternatives to Cow’s Milk-Based Infant Formulas in the Prevention and Management of Cow’s Milk Allergy

Maryniak

Sancho

Hansen

et al. 2022

Foods

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Cow’s milk-based infant formulas are the most common substitute to mother’s milk in infancy when breastfeeding is impossible or insufficient, as cow’s milk is a globally available source of mammalian proteins with high nutritional value. However, cow’s milk allergy (CMA) is the most prevalent type of food allergy among infants, affecting up to 3.8% of small children. Hypoallergenic infant formulas based on hydrolysed cow’s milk proteins are commercially available for the management of CMA. Yet, there is a growing demand for more options for infant feeding, both in general but especially for the prevention and management of CMA. Milk from other mammalian sources than the cow, such as goat, sheep, camel, donkey, and horse, has received some attention in the last decade due to the different protein composition profile and protein amino acid sequences, resulting in a potentially low cross-reactivity with cow’s milk proteins. Recently, proteins from plant sources, such as potato, lentil, chickpeas, quinoa, in addition to soy and rice, have gained increased interest due to their climate friendly and vegan status as well as potential lower allergenicity. In this review, we provide an overview of current and potential future infant formulas and their relevance in CMA prevention and management.

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“…The calculation of DH was outlined previously (Sheng et al, 2021). The maximal concentration of free amines was obtained by hydrolyzing the protein solutions before digestion in 6 M HCl at 110°C for 24 h (Halabi et al, 2020;Sousa et al, 2020).…”

Section: Degree Of Hydrolysismentioning

confidence: 99%

Effects of genetic variants and sialylation on in vitro digestibility of purified κ-casein

Sheng

Nielsen

Glantz

et al. 2022

Journal of Dairy Science

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Milk with different κ-casein (CN) phenotypes has previously been found to influence its gastric digestion rate. Therefore, the aim of the present study is to disentangle contributions of genetic variation and its related sialylation on the in vitro digestion process of κ-CN. Accordingly, κ-CN was purified from milk representing homozygous cows with κ-CN phenotypes AA, BB, or EE and used as substrate molecules in model studies using the INFOGEST 2.0 in vitro static digestion model. Furthermore, the effect of removal of the terminal sialic acids present on the O-linked oligosaccharides of the purified κ-CN A, B, and E protein variants were studied by desialylation enzymatic assays. The κ-CN proteins were purified by reducing anion exchange chromatography with purities of variants A, B, and E of 93.0, 97.1, and 90.0%, respectively. Protein degradations of native and desialylated κ-CN isolates in gastric and intestinal phases were investigated by sodium dodecylsulphate-PAGE, degree of hydrolysis (DH), and liquid chromatography electrospray ionization mass spectrometry. It was shown that after purification, the κ-CN molecules reassembled into multimer states, which then constituted the basis for the digestion studies. As assessed by DH, purified variants A and E were found to exhibit faster in vitro digestion rates in both gastric and intestinal phases compared with variant B. Desialylation increased both gastric and intestinal digestion rates for all variants, as measured by DH. In the gastric phase, desialylation promoted digestion of variant B at a rate comparable with native variants A and E, whereas in the intestinal phase, desialylation of variant B promoted better digestion than native A or E. Taken together, the results confirm that low glycosylation degree of purified κ-CN promotes faster in vitro digestion rates, and that desialylation of the O-linked oligosaccharides further promotes digestion. This finding could be applied to produce dairy products with enhanced digestibility.

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Modification of protein structures by altering the whey protein profile and heat treatment affectsin vitrostatic digestion of model infant milk formulas

Abstract: The aim was to investigate how protein structures in model infant milk formulas affect proteolysis kinetics during in vitro digestion.

Cited by 54 publications

References 65 publications

Impact of alfalfa (Medicago sativa L.) galactomannan on the microstructural and physicochemical changes of milk proteins under static in-vitro digestion conditions

Impact of alfalfa (Medicago sativa L.) galactomannan on the microstructural and physicochemical changes of milk proteins under static in-vitro digestion conditions

Alternatives to Cow’s Milk-Based Infant Formulas in the Prevention and Management of Cow’s Milk Allergy

Effects of genetic variants and sialylation on in vitro digestibility of purified κ-casein

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