Research on milk fat globule membrane (MFGM) is gaining traction. The interest is two-fold; on the one hand, it is a unique trilayer structure with specific secretory function. On the other hand, it is the basis for ingredients with the presence of phospho- and sphingolipids and glycoproteins, which are being used as food ingredients with valuable functionality, in particular, for use as a supplement in infant nutrition. This last application is at the center of this Review, which aims to contribute to understanding MFGM’s function in the proper development of immunity, cognition, and intestinal trophism, in addition to other potential effects such as prevention of diseases including cardiovascular disease, impaired bone turnover and inflammation, skin conditions, and infections as well as age-associated cognitive decline and muscle loss. The phospholipid composition of MFGM from bovine milk is quite like human milk and, although there are some differences due to dairy processing, these do not result in a chemical change. The MFGM ingredients, as used to improve the formulation in different clinical studies, have indeed increased the presence of phospholipids, sphingolipids, glycolipids, and glycoproteins with the resulting benefits of different outcomes (especially immune and cognitive outcomes) with no reported adverse effects. Nevertheless, the precise mechanism(s) of action of MFGM remain to be elucidated and further basic investigation is warranted.

Copyright © 2014. . © 2014 Conway, Gauthier, and Pouliot

When mother's milk is insufficient, pasteurized human donor milk (DM) is the recommended supplement for hospitalized very-low-birth-weight infants. The current method of pasteurization (Holder, 62.5°C, 30 min) negatively affects heat-sensitive nutrients and bioactive proteins. Objectives of this study were to compare changes in DM composition after thermal pasteurization (Holder and flash-heating) and nonthermal methods [UV-C irradiation and high hydrostatic pressure (HHP)]. We hypothesized that nonthermal techniques would result in fewer changes to composition. Holder, flash-heating (brought to boil), UV-C irradiation (250 nm, 25 min), and HHP (500 MPa, 8 min) were studied. Pools of milk from 17 women known to contain bacteria at >5 × 107 colony forming units (CFU)/L were collected from the Rogers Hixon Ontario Human Milk Bank and underwent each pasteurization technique. Macronutrients, heat-sensitive micronutrients (vitamin C, folate), and bioactive components [bile-salt-stimulated lipase (BSSL), lysozyme, lactoferrin] were measured in raw and pools of pasteurized milk. Milk was cultured to determine how well each technique produced a culture negative result (detection limit <1 × 103 CFU/L). Folate was reduced by 24-27% after Holder, flash-heating, and UV-C (P < 0.05); no reduction was observed after HHP. All pasteurization methods reduced vitamin C (60-75%, P < 0.001). BSSL was abolished after Holder and flash-heating (P < 0.001), reduced after UV-C (48%, P < 0.001), but unaffected by HHP. Lysozyme activity was reduced after flash-heating (44%) and UV-C (74%, P < 0.004) but unaffected by Holder or HHP. Lactoferrin was reduced by all methods (P < 0.02) but most severely by flash-heating (74%) and least severely by HHP (25%). Holder and UV-C reduced lactoferrin by ∼48%. All pasteurization methods reduced the number of culture positive DM samples (P < 0.001). HHP better preserves human milk composition than Holder pasteurization. Future research on the feasibility of HHP for pasteurizing human milk is warranted because its implementation may improve the nutritional status and health of DM-fed infants.

Edible insects have garnered increased interest as alternative protein sources due to the world’s growing population. However, the allergenicity of specific insect proteins is a major concern for both industry and consumers. This preliminary study investigated the capacity of high hydrostatic pressure (HHP) coupled to enzymatic hydrolysis by Alcalase^® or pepsin in order to improve the in vitro digestion of mealworm proteins, specifically allergenic proteins. Pressurization was applied as pretreatment before in vitro digestion or, simultaneously, during hydrolysis. The degree of hydrolysis was compared between the different treatments and a mass spectrometry-based proteomic method was used to determine the efficiency of allergenic protein hydrolysis. Only the Alcalase^® hydrolysis under pressure improved the degree of hydrolysis of mealworm proteins. Moreover, the in vitro digestion of the main allergenic proteins was increased by pressurization conditions that were specifically coupled to pepsin hydrolysis. Consequently, HHP-assisted enzymatic hydrolysis represents an alternative strategy to conventional hydrolysis for generating a large amount of peptide originating from allergenic mealworm proteins, and for lowering their immunoreactivity, for food, nutraceutical, and pharmaceutical applications.

High-milk-protein concentrates (>80% on a dry weight basis) are typically produced by ultrafiltration (UF) with constant-volume diafiltration (DF). To maximize protein retention at a commercial scale, polymeric spiral-wound UF membranes with a molecular weight cut-off (MWCO) of 10 kDa are commonly used. Flux decline and membrane fouling during UF have been studied extensively and the selection of an optimal UF-DF sequence is expected to have a considerable effect on both the process efficiency and the volumes of by-products generated. The objective of this study was to characterize the performance of the UF-DF process by evaluating permeate flux decline, fouling resistance, energy and water consumption, and retentate composition as a function of MWCO (10 and 50 kDa) and UF-DF sequence [3.5×-2 diavolumes (DV) and 5×-0.8DV]. The UF-DF experiments were performed on pasteurized skim milk using a pilot-scale filtration system operated at 50°C under a constant transmembrane pressure of 465 kPa. The results showed that MWCO had no effect on permeate flux for the same UF-DF sequence. Irreversible resistance was also similar for both sequences, whatever the MWCO, suggesting that soluble protein deposition within the pores is similar for all conditions. Despite lower permeate fluxes and greater reversible resistance for the 5×-0.8DV sequence, the overall energy consumption of the 2 UF-DF sequences was similar. However, the 3.5×-2DV sequence required more water for DF and generated larger volumes of permeate to be processed, which will require more membrane area and lead to greater environmental impact. A comparative life cycle assessment should however be performed to confirm which sequence has the lowest environmental impact.