Improving ultrafiltration efficiency of acidified skim milk using bipolar membrane electrodialysis: Impact on protein concentrate composition, process performance, and fouling.

The efficiency of ultrafiltration (UF) of acidified skim milk (SM) is impaired by protein aggregation and mineral scaling. The aim of this study is to assess the potential of acidification by electrodialysis with bipolar membranes (EDBM), in comparison with citric acid (CA), prior to the UF process on filtration performance, fouling and composition of the protein concentrates. Electro-acidification, facilitated by a water-splitting reaction, decreased the pH of milk to ∼ 5.

Development of a human milk protein concentrate from donor milk: Impact of the pasteurization method on static in vitro digestion in a preterm newborn model.

The impact of high temperature short time (HTST, 72 °C, 15 s), Holder pasteurization- (63 °C, 30 min) and high hydrostatic pressure (HHP, 600 MPa-10 min) was evaluated on the digestibility of human milk protein concentrate (HMPC) by using a static in vitro gastrointestinal digestion system. The results showed that the processing steps used to produce the HMPC induced a decrease in readily available nitrogen (non-protein nitrogen and peptides). Overall, digestibility was similar between pasteurized and raw HMPC (degree of hydrolysis ranged from 26 to 34 %).

Impact of holder, high temperature short time and high hydrostatic pressure pasteurization methods on protein structure and aggregation in a human milk protein concentrate.

This work evaluated the impact of high temperature short time (HTST, 72 °C, 15 s), high hydrostatic pressure (HHP, 400-600 MPa at 5 and 10 min) and Holder pasteurization (HoP, 62.5 °C, 30 min) on protein profile and aggregation in a human milk protein concentrate (HMPC). The structural changes induced in milk proteins were investigated in HMPC as well as in sedimentable and non-sedimentable fractions recovered after ultracentrifugation.

Occurrence of Peptide-Peptide Interactions during the Purification of Self-Assembling Peptide f1-8 from a β-Lactoglobulin Tryptic Hydrolysate.

Self-assembling peptides have gained attention because of their nanotechnological applications. Previous work demonstrated that the self-assembling peptide f1-8 (Pf1-8) that is generated from the tryptic hydrolysis of β-lactoglobulin can form a hydrogel after several purification steps, including membrane filtration and consecutive washes. This study evaluates the impact of each processing step on peptide profile, purity, and gelation capacity of each fraction to understand the purification process of Pf1-8 and the peptide-peptide interactions involved.

A Human Milk-Based Protein Concentrate Developed for Preterm Infants Retains Bioactive Proteins and Supports Growth of Weanling Rats.

Background: Bovine milk-based protein modulars are currently available to nutrient-enrich enteral feedings; however, they have limitations for use in very-low-birth-weight infants.

Objectives: Our objectives were to develop a human milk-based protein (HMP) concentrate and to conduct a preclinical assessment of the HMP concentrate in weanling rats.

Methods: An HMP concentrate was produced from donor milk using pressure-driven membrane filtration processes and high hydrostatic pressure processing.

The ultrafiltration molecular weight cut-off has a limited effect on the concentration and protein profile during preparation of human milk protein concentrates.

Optimizing protein intake for very low birth weight (<1,500 g) infants is fundamental to prevent faltering postnatal growth with the potential association of impaired neurodevelopment. The protein content of human milk is not sufficient to support the growth of very low birth weight infants. To meet their elevated protein requirements, human milk is currently fortified using typically bovine milk-based protein isolates (>85% on a dry basis).

Production of highly purified fractions of α-lactalbumin and β-lactoglobulin from cheese whey using high hydrostatic pressure.

Despite extensive research on the topic, valorization of dairy by-products remains challenging. Cheese whey is of particular interest because it contains valuable proteins such as α-lactalbumin (α-LA) and β-lactoglobulin (β-LG). However, selective fractionation of these 2 proteins into pure fractions is complex because of their similar molecular weights.

High hydrostatic pressure induced extraction and selective transfer of β-phosvitin from the egg yolk granule to plasma fractions.

Egg yolk phosvitin is of particular interest due to its functional and biological properties. Recently, it was demonstrated that high hydrostatic pressure (HHP) (400 MPa for 5 min) induced the transfer of folic acid and phosvitin from the egg yolk granule to the plasma fraction. A granule fraction (G) produced by egg yolk centrifugation was pressure-treated at 400 and 600 MPa for 5 and 10 min, and centrifuged to generate granule fractions (G to G) and plasmas (P to P).

Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure.

Fractionation of β-lactoglubulin (β-lg) and α-lactalbumin (α-la) using conventional separation technologies remains challenging mainly due to similar molecular weight. Herein, casein (CN) was used as ligand protein to specifically aggregate β-lg under high hydrostatic pressure (HHP) in order to separate α-la after acidification to pH 4.6.

Formation of Stable Supramolecular Structure with β-Lactoglobulin-Derived Self-Assembling Peptide f1-8 and Bovine Micellar Caseins.

The development of stable macromolecular structures with tailored functional properties in the dairy industry using innovative stabilizers is of great interest. The self-assembling peptide f1-8 (Pf1-8) derived from β-lactoglobulin was found to interact with whey proteins, consequently changing their physicochemical properties. The objective of the present work was to evaluate the interaction between Pf1-8 and micellar casein (CN) and the changes in their physicochemical properties and stability at different pH values (6.

High hydrostatic pressure-assisted enzymatic hydrolysis improved protein digestion of flaxseed protein isolate and generation of peptides with antioxidant activity.

Exploration of innovative high hydrostatic pressure (HHP)-assisted enzymatic hydrolysis of plant based food proteins may help improve peptide yield and bioactivity of hydrolysates. In this study, we performed enzymatic hydrolysis of flaxseed proteins using trypsin under HHP (100 and 300 MPa for 5 and 10 min) to evaluate the effect of presurization on protein denaturation, degree of hydrolysis (DH), and peptide profile and bioactivity of hydrolysate. Spectrofluorimetric analyses showed that 300 MPa induced the maximum destablization of flaxseed protein structures.