During storage, some factors (for example, storage duration and temperature) can affect milk stability and consumer acceptability. Thiobarbituric acid reactive substances (TBARSs), lipid classes, and fatty acid profiles in stored ultra‐high temperature (UHT) milk were analyzed to assess the effects of storage time and temperature on lipid oxidation and lipolysis. With storage duration up to 12 months, the milk fat phase was separated and showed high levels of oxidation and lipolysis, manifested as increased levels of TBARS and free fatty acids. High oxidation levels decreased the percentage of unsaturated fatty acids (UFAs) in triacylglycerol and phospholipids. Higher storage temperatures (20, 30, and 37 °C) resulted in a higher degree of fat aggregation, oxidation, and lipolysis compared with refrigerated storage (4 °C). Additionally, sampling month of raw milk (May, July, and November) affected the lipid profiles of UHT milk during storage, with more UFA oxidized in July than in the other 2 months.

Protein nanofibrils (PNFs) have potential for use in food applications as texture inducers. This study investigated the formation of PNFs from protein extracted from whole fava bean and from its two major storage proteins, globulin fractions 11S and 7S. PNFs were formed by heating (85 °C) the proteins under acidic conditions (pH 2) for 24 h. Thioflavin T fluorescence and atomic force microscopy techniques were used to investigate PNF formation. The foaming properties (capacity, stability, and half-life) were explored for non-fibrillated and fibrillated protein from fava bean, 11S, and 7S to investigate the texturing ability of PNFs at concentrations of 1 and 10 mg/mL and pH 7. The results showed that all three heat-incubated proteins (fava bean, 11S, and 7S) formed straight semi-flexible PNFs. Some differences in the capacity to form PNFs were observed between the two globulin fractions, with the smaller 7S protein being superior to 11S. The fibrillated protein from fava bean, 11S, and 7S generated more voluminous and more stable foams at 10 mg/mL than the corresponding non-fibrillated protein. However, this ability for fibrillated proteins to improve the foam properties seemed to be concentration-dependent, as at 1 mg/mL, the foams were less stable than those made from the non-fibrillated protein.

Faba beans, rich in protein and ideal for Swedish cultivation, are limited in food industry use due to anti-nutritional factors (ANFs) that hinder nutrient absorption. An extraction method was developed in our study to mitigate ANFs in faba beans, using aqueous alkaline methods and isoelectric precipitation with differential salt concentration. This method yielded 15.8 g of protein per 100 g of flour, with a protein concentration exceeding 83% of the total extract. It reduced ANFs like phytic acid (28.0%), lectins (87.5%), vicine (98.5%), and convicine (99.7%). Extraction conditions were optimized using response surface methodology, identifying pH 6, 2 h, and 20 °C as the most effective parameters, achieving an 86% reduction in phytic acid, closely matched the model's predictions (R² = 0.945). This method effectively reduced ANFs, offering a sustainable approach for producing proteins suitable for diverse food products, including plant-based alternatives.