Buttermilk is a potential material for the production of a milk fat globule membrane (MFGM) and can be mainly classified into two types: whole cream buttermilk and cheese whey cream buttermilk (WCB). Due to the high casein micelle content of whole cream buttermilk, the removal of casein micelles to improve the purity of MFGM materials is always required. This study investigated the effects of rennet and acid coagulation on the lipid profile of buttermilk rennet-coagulated whey (BRW) and buttermilk acid-coagulated whey (BAW) and compared them with WCB. BRW has significantly higher phospholipids (PLs) and ganglioside contents than BAW and WCB. The abundance of arachidonic acid (ARA)- and eicosapentaenoic acid (EPA)-structured PLs was higher in WCB, while docosahexaenoic acid (DHA)-structured PLs were higher in BRW, indicating that BRW and WCB intake might have a greater effect on improving cardiovascular conditions and neurodevelopment. WCB and BRW had a higher abundance of plasmanyl PL and plasmalogen PL, respectively. Phosphatidylcholine (PC) (28:1), LPE (20:5), and PC (26:0) are characteristic lipids among BRW, BAW, and WCB, and they can be used to distinguish MFGM-enriched whey from different sources.

The effect of whey proteins and heat treatment (90 °C, 5 min) on pepsin-induced hydrolysis of κ-casein, and subsequent coagulation of casein micelles, was investigated at pH 6.3 and 6.0 using reverse-phase HPLC, oscillatory rheology, and confocal laser scanning microscopy. Whey proteins did not affect the hydrolysis of κ-casein but retarded the coagulation process. Heat treatment did not affect the hydrolysis kinetics in whey protein (WP)-free samples, but slightly impaired the hydrolysis rate in WP-containing samples. The coagulation process of WP-free samples was little affected by heat-treatment. However, compared with unheated WP-contained sample at the same pH, the coagulation process of the heated sample was retarded at pH 6.3 but enhanced at pH 6.0. The curd in heated samples with smaller pores had higher water holding capacity. This knowledge provides further understanding on the role of whey proteins and heat treatment on the coagulation mechanisms of milk under gastric conditions.

Processing of milk involves heating, which can modify the structure and digestibility of its proteins. In vitro models are useful for studying protein digestion. However, validating these models with in vivo data is challenging. Here, we non-invasively monitor in vitro gastric milk protein digestion by protein-water chemical exchange detected by 1H nuclear magnetic resonance (NMR) magnetization transfer (MT). We obtained either a fitted composite exchange rate (CER) with a relative standard error of ≤10% or the MT ratio (MTR) of the intensity without or with an off-resonance saturation pulse, from just a single spectral acquisition. Both CER and MTR, affected by the variation in the amount of semi-solid protons, decreased during in vitro gastric digestion in agreement with standard protein content analyses. The decrease was slower in heated milk, indicating slower breakdown of the coagulum. Our results open the way to future quantification of protein digestion in vivo by MRI.