The aim of this study was to concentrate whey protein by ultrafiltration process, evaluating the pressure at 1–3 bar and temperature of 10–20℃. In the conditions that show the more protein concentration were evaluated the interfacial and emulsifying properties at pH 5.7 and 7.0. The whey concentrate at 10℃ and 1.5 bar showed the higher protein value 36% (w/w), with soluble protein of 33.82% (solubility of 93.94%) for pH 5.7 and 34% (solubility of 94.4%) for pH 7.0, respectively. The whey concentrate powder present particle size distribution between 0.4-110 um. The whey at pH 5.7 and 7.0 was not observed significant differences in the resistance parameters of the oil/water layer interface. The interfacial film formed by the proteins presented an essentially elastic behavior in both pH, and in pH 5.7 the emulsion was more stable with lower diameter droplets. The concentrate whey showed techno-functional properties (emulsification and solubility), which allow the use as ingredients in products of industrial interest in food products such as mayonnaise, ice cream, sauces, and others.

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The objective of this study is to elaborate Serra da Estrela cheese with sheep's milk concentrate by ultrafiltration and characterize it in relation to protein, yield, proteolysis, amino acid profile, and acceptability. The cheese elaborated with concentrate milk (F2) presented an increase of 17% yield, and protein content was 2 times higher than cheese without concentrate milk (F1). On the 30thday of storage F2 presented an increase of the amino acids and also of proteolysis extension and depth index in relation to the 1st day. Also presented better sensorial characteristic in relation to F1. Were observed positive correlations (>0.85) between acceptability in relation to protein, depth index, extensionand extension index, valine, methionine, serine, phenylalanine aspartic acid, valine andproline. Cheese elaborated with concentrate milk and coagulated with thistle flower is one alternative to increase cheese yield with differential sensorial characteristics.

Rice bran is a by-product of the rice milling process, found worldwide in abundance and highlighted due its protein content. This study optimized the conditions for ultrasonic-assisted extraction of protein from defatted rice bran (DRB) and characterized the rice bran protein concentrate (RBPC). A sequential strategy of experimental design was employed; the effect of pH, temperature, ultrasound exposure time, and amplitude were evaluated regarding the percentage of protein extraction by a Full factorial design (FFD) with a fixed frequencies (FFD-A: 37 kHz; FFD-B: 80 kHz). Subsequently, the percentage of protein extracted was optimized employing a Central composite rotatable design (variables: pH and ultrasound exposure time) and RBPC obtained was characterized regarding chemical and functional properties. The pH and ultrasound exposure time had positive effect (P ≤ 0.05) on percentage of protein extraction; moreover, 37 kHz frequency was more effective in protein extraction. The optimized condition (frequency: 37 kHz; temperature: 30 °C; pH: 10; ultrasound exposure time: 30 min; and amplitude: 100%) allowed 15.07% of protein recovery and the RBPC presented 84.76 g 100 g-1 of protein. Magnesium and copper were the main mineral in RBPC (34.4 and 25.5 µg g-1, respectively), while leucine was the limiting amino acid (0.42) and threonine presented the highest chemical score (1.0). The RBPC solubility was minimal at pH 4 and higher at pHs 6-10; the water and oil absorption capacity were higher than bovine serum albumin (BSA) and the emulsifying capacity was comparable to BSA, with a suitable stability. It was possible to obtain a higher purity RBPC than described in the literature, due to the optimization in the extraction process steps, with functional properties suitable for application in food products, especially emulsified ones.

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Aqueous two-phase systems (ATPS) stand out as an alternative technique for recovering and concentrating proteins. However, the study of ATPS to recover Arthrospira platensis protein is still poorly reported. This research used a sequential strategy of experimental design to evaluate the protein recovery from A. platensis protein extract using ATPS composed of polyethylene glycol (PEG: 1500, 4000, 6000, and 8000 Da) and saline solution (potassium phosphate and sodium citrate). The maximized conditions for A. platensis protein recovery were established by using 16% sodium citrate and 18% PEG 1500 Da, reaching 1.02 of purification factor and 75% protein recovery. Electrophoresis analysis showed protein bands between 5 and 15 kDa, characteristic size of phycobiliproteins. PEG and sodium citrate ATPS are a simple and low-cost alternative to the recovery A. platensis protein and show potential for industrial application.