Most potato proteins are fractions of albumin and globulin, soluble in water and in water and salt solutions, respectively; these are patatin glycoproteins, with a pIs in the range of 4.8–5.2. This group of proteins is typical of potato and they are referred to as patatin or tuberin. Around 30–50% of soluble potato proteins comprise numerous fractions of protease inhibitors with a molecular weight in the range of 7–21 kDa; they are often heat-resistant, showing a wide spectrum of health-promoting effects. The nutritional value of proteins is related to the content of amino acids, their mutual proportions and digestibility. Natural proteins of the patatin fraction are characterized by favorable functional properties, including foam formation and stabilization, fat emulsification or gelling. Native potato proteins may also exhibit beneficial non-food properties, such as antimicrobial or antitumor, as well as antioxidant and antiradical. Depending on the method of isolation and the applied factors, such as pH, ionic strength and temperature, the directions of using potato protein preparations will be different.

Opuntia ficus-indica (L.) Mill. is the Cactaceae plant with the greatest economic relevance in the world. It can be used for medicinal purposes, animal nutrition, production of biofuels and phytoremediation of soils. Due to its high content of bioactive compounds, the prickly pear has antioxidant, antimicrobial and anticancer properties. The aim of this study was to determine the polyphenolic, fatty acid and amino acid profile and characterize the antioxidant capacity of seeds of seven Spanish prickly pear cultivars. A total of 21 metabolites, mainly phenolic acids and flavonols, were identified using ultraperformance liquid chromatography photodiode detector quadrupole/time-of-flight mass spectrometry (UPLC-PDA-Q/TOF-MS). Significant differences were found in the phenolic concentrations of the investigated varieties. The highest amount of phenolic compounds (266.67 mg/kg dry matter) were found in the “Nopal espinoso” variety, while the “Fresa” variety was characterized by the lowest content (34.07 mg/kg DM) of these compounds. In vitro antioxidant capacity was positively correlated with the amount of polyphenols. The amino acid composition of protein contained in prickly pear seeds was influenced by the variety. Glutamic acid was the predominant amino acid followed by arginine, aspartic acid and leucine, independent of prickly pear variety. Overall, 13 different fatty acids were identified and assessed in prickly pear seeds. The dominant fatty acid was linoleic acid, with content varying between 57.72% “Nopal ovalado” and 63.11% “Nopal espinoso”.

Buckwheat by-products may be used as promising food ingredients due to their nutritional composition. Buckwheat husk (BH) may be used in meat products as a source of valuable compounds. In this study, the addition of BH to the quality of frankfurter-type sausages was investigated, aiming to reduce buckwheat waste and to develop nutritionally enriched sausages. For the purpose of this study, a range of measurements, as well as observations, have been carried out. This included the following: pH, weight losses, yield, the instrumental color and texture measurement, protein digestibility, polyphenols, amino acid, trace elements analysis, and the organoleptic evaluation. Compared with no BH sausages, the cooking losses of sausages with 3% BH were higher, while storage losses were lower. BH increased the hardness of sausages after two weeks of storage. The growing addition of BH resulted in a decrease in L* and b*. This change of color resulted in its lower level of consumer acceptability. BH addition did not reduce the protein digestibility. The total amino acid content increased with the increasing husk addition, from 161.8 mg/kg to 228.0 mg/kg. Moreover, BH increased the content of manganese, calcium, potassium and magnesium. This research suggested that incorporation of BH improved the nutritional value of sausages with minimal changes in technological and sensory properties.

The purpose of the present study was to determine the effects of acetylation with different doses of acetic anhydride on the chemical composition and chosen functional properties of commercial pumpkin protein concentrate (PPC). The total protein content decreased as compared to unmodified samples. Electrophoretic analysis revealed that in the acetylated pumpkin protein, the content of the heaviest protein (35 kDa) decreased in line with increasing concentrations of modifying reagent. Acetylation of PPC caused a significant increase in water-binding and oil-absorption capacity and for emulsifying properties even at the dose of 0.4 mL/g. Additionally, an increase in foaming capacity was demonstrated for preparations obtained with 2.0 mL/g of acetic anhydride, whereas acetylation with 0.4 and 1.0 mL/g caused a decrease in protein solubility as compared to native PPC.

The aim of the present study was to increase the value of rice protein concentrate (RPC) by improving the functional properties of a preparation subjected to acetylation and analyze the impact of this chemical modification on chemical composition, digestibility, and protein patterning using SDS-PAGE electrophoresis and FT-IR spectroscopy. In the modified samples, the protein content increased (80.90–83.10 g/100 g cf. 74.20 g/100 g in the control). Electrophoresis revealed that the content of the main rice protein fractions (prolamin and glutelin) decreased as the concentration of the modifying reagent increased. Through spectroscopic analysis, wavenumbers, corresponding to the presence of proteins or lipids, aromatic systems, and carbohydrates, were observed. The use of acetic anhydride did not change the digestibility of the modified RPC significantly when compared to that of the control sample. The acetylation of the RPC caused a significant increase in its emulsifying properties at pH 8 (1.83–14.74%) and its water-binding capacity but did not have a statistically significant impact on the oil-absorption capacity. There was a slight increase in protein solubility and a decrease in foaming capacity in the modified RPC.