Nectarine powder of Bulgarian origin: Physicochemical composition, antioxidant activity, microbiological and sorption characteristics.

One way to improve the quality of food products is by conducting more thorough research on regional foods. This approach has several benefits, such as promoting human health, supporting the local economy, and preserving cultural food traditions. In this regard, our study investigated the potential of nectarine powder as a regional fruit product that could be developed into a global innovation. The present study examined: the physicochemical composition, antioxidant activity, microbiological load, and adsorption and desorption characteristics of the nectarine powder. The fruit powder was acquired through the use of a heat pump dryer, where drying took place at 42 °C for a duration of 8 h until achieving a moisture content ranging from 13.5 % to 14.5 %. The approximate physicochemical values are as follows: proteins, total carbohydrates, crude fiber, ash content and total lipids. Microbiological parameters, namely the total count of mesophilic aerobic and facultative anaerobic microorganisms, yeasts and molds, Escherichia coli, Salmonella spp., coagulase-positive staphylococci, and coliforms were checked and found to be within the acceptable limits as stipulated by the relevant state standards. Antioxidant activity was demonstrated through the utilization of various methods, including DPPH (33.19 ± 0.09mMTE/g extract), ABRS (2.55 ± 0.05mMTE/g extract), FRAP (1.43 ± 0.03mMTE/g extract) and CUPRAC (0.83 ± 0.01mMTE/g extract) methods. Investigation of the mass transfer sorption characteristics is performed using the gravimetric-static method. The conditions of the experiment were selected according to the usual conditions in which the food products are found in the commercial depot. The equilibrium and monolayer moisture data are investigated at 10 °C, 25 °C and 40 °C and relative air humidity in the wide range from 11 % to 87 %, achieved by the salts saturated solutions. To depict the adsorption and desorption isotherms, the modified models of Halsey, Chung-Pfost, Henderson, and Oswin were selected.

Green Assessment of Phenolic Acid Composition and Antioxidant Capacity of Advanced Potato Mutant Lines through UPLC-qTOF-MS/MS Quantification.

Potatoes are one of the most consumed crops worldwide. They contain a high amount of bioactive compounds such as phenolic compounds and vitamins with important antioxidant activities, which makes this crop of high biological value for human health. The goal of this research was to biochemically evaluate polyphenol levels and antioxidant capacities in parent and control genotypes compared to advanced mutant potato lines in the M1V8 generation. This will reveal the genetic changes that result from induced mutagenesis. The quantified compounds and the evaluated antioxidant activity boost the health benefits of consuming the improved mutant potatoes. In the present study, the phenolic composition and antioxidant activity of eighteen mutant and initial potato genotypes were analyzed by UPLC-qTOF-MS/MS and the ORAC method, respectively. In each of the hybrid combinations, mutant lines with an improved phenolic compound profile were observed. Representative samples from the third hybrid combination had notable increases in phenolic compound concentrations, as well as the presence of metabolites not found in the parental lines. With one exception, the remaining nine mutants showed significantly higher antioxidant capacities. The results will be used in future potato breeding programs, with participation of the valuable mutant lines containing new phenolic substances not present in the initial genotypes.

Value-Added Dietary Fiber Concentrate Obtained as Waste after Protein Isolation from Ethanol-Treated Sunflower Meal.

Deproteinized sunflower meal (DSM) was obtained as waste from ethanol-treated sunflower meal after alkaline extraction of proteins. The study aimed at biochemically and functionally characterizing the material concerning its potential practical application and valuability. The DSM consisted mainly of proteins (19.88%) and dietary fibers (61.06%) the majority of which were insoluble (53.09%). Cellulose (30.87%) and lignin (21.79%) were the most contributing compounds to the total amount of dietary fibers. The DSM contained Fe (133.29 mg/kg), Zn (201.56 mg/kg), and Cu (31.87 mg/kg). The analyses defined the DSM as a fiber concentrate with relatively high thermal stability. The distraction of the material began at 170°Ð¡ with a maximum speed at 277°Ð¡. The highest water absorption capacity (WAC) of the DSM was observed at pH 6 and 7 (approximately 8 g H2O/g sample) under all studied conditions including pH from 3 to 10 and three levels of NaCl concentrations (0.00 M, 0.03 M, and 0.25 M). At pH 7, increasing temperature from 20°C to 60°C increased the WAC of the DSM from 8.13 g H2O/g sample to 9.80 g H2O/g sample, respectively. Further increase in the temperature diminished the WAC of the DSM. At pH 6, the increase in temperature did not influence positively the WAC of the DSM. The study demonstrated the potential of the DSM, a waste obtained from the protein isolation process, as a valuable ingredient/additive in the food industry.

Multifunctionality of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation.

Rapeseed meal is a by-product of the oil-producing industry with a currently underestimated application. Two protein isolates, PI2.5-8.5 or PI10.5-2.5, were obtained from industrial rapeseed meal after treatment with an aqueous ethanol solution. The alkaline-extracted proteins were sequentially precipitated by two different modes, from pH 10.5 to 2.5, and vice versa, from 2.5 to 8.5, with a step of 1 pH unit. The preparation approach influenced both the functional and antioxidant properties of the isolates. The PI10.5-2.5 exhibited higher water and oil absorption capacities than PI2.5-8.5, reaching 2.68 g H2O/g sample and 2.36 g oil/g sample, respectively. The emulsion stability of the PI2.5-8.5, evaluated after heating at 80 °C, was either 100% or close to 100% for all pH values studied (from 2 to 10), except for pH 6 where it reached 93.87%. For the PI10.5-2.5, decreases in the emulsion stability were observed at pH 8 (85.71%) and pH 10 (53.15%). In the entire concentration range, the PI10.5-2.5 exhibited a higher scavenging ability on 2,2-diphenyl-1-picryl hydrazyl (DPPH) and hydroxyl radicals than PI2.5-8.5 as evaluated by DPPH and 2-deoxyribose assays, respectively. At the highest concentration studied, 1.0%, the neutralization of DPPH radicals by PI10.5-2 reached half of that exhibited by synthetic antioxidant butylhydroxytoluene (82.65%). At the same concentration, the inhibition of hydroxyl radicals by PI10.5-2 (71.25%) was close to that achieved by mannitol (75.62%), which was used as a positive control. Established antioxidant capacities add value to the protein isolates that can thus be used as both emulsifiers and antioxidants.

Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation.

The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5-2.5 and PI2.5-8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5-8.5 contained a higher amount of crude protein (72.84%) than PI10.5-2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5-2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5-2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5-8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5-2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5-8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5-8.5, while the solubility of PI10.5-2.5 was increased. The supplementation of PI10.5-2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates.

Stability of sunflower and rapeseed oil-in-water emulsions supplemented with ethanol-treated rapeseed meal protein isolate.

A protein isolate (ERPI) was prepared from ethanol-treated rapeseed meal and used as a stabilizing agent in sunflower and rapeseed oil-in-water emulsions. The aim of the current study was to explore the influence of protein and oil concentrations on initial stability of sunflower and rapeseed oil-in-water emulsions by evaluating Gibbs free energy (ΔG) and particle size distribution. The 7-day dynamics of emulsion stability was investigated by turbidity measurement as well. A 32 factorial design was applied to assess the significance of oil (5%, 10% and 15% w/w) and ERPI protein (0.25%, 0.5% and 1.0% w/w) addition on stability of the emulsions. The results demonstrated that the increase of oil concentrations from 5 to 15% positively influenced the initial stability of sunflower and rapeseed oil-in-water emulsions. In both oil types, ERPI protein supplementation at all levels resulted in significant differences in the stability of 5% and 10% oil emulsions but did not alter the initial stability of the emulsions prepared with either 15% sunflower or rapeseed oil. With a few exceptions, there was a good agreement between Gibbs free energy data and microstructural profiles of the emulsions. Overall, emulsions with all sunflower oil concentrations and 1.0% ERPI protein exhibited better initial and a 7-day stability dynamics compared to all rapeseed oil-based emulsions. The study demonstrated the potential of ethanol-treated rapeseed meal protein isolate to serve as an emulsifying agent in sunflower and rapeseed oil containing emulsions.

Foaming properties of acid-soluble protein-rich ingredient obtained from industrial rapeseed meal.

The use of the rapeseed meal as a source for preparation of protein-rich ingredients for the food industry is an alternative to the current limited application as a feed additive. The aim of this study was to evaluate foaming properties of an acid-soluble protein-rich ingredient (ASP) obtained from industrial rapeseed meal as a co-product of a protein isolate. Foam capacity and stability over a period of 60 min were evaluated by using volumetric and image analyzing methods. The influence of NaCl at two boundary concentrations (0.03 and 0.25 M) was studied over a pH range from 2 to 10. The ASP exhibited high foamability (> 90%), not influenced by pH or salt addition. In contrast, foam stability, measured over a 60 min period, was pH and NaCl dependent. By the end of the observation period, the addition of 0.25 M NaCl reduced the foam volume by more than 70% at all pH values. After 30 min at pH values 4, 6 and 8, which are the most common for food products, the foams without NaCl retained 51, 38 and 41% of the initial foam volume, respectively. The results were in agreement with image analysis observations where microstructure of the foams with NaCl was more heterogeneous than that of the foams without salt addition. The high foamability and relatively high foam stability at pH from 4 to 8 without NaCl addition shows that ASP could be a potential alternative to plant proteins currently used as foaming agents in the food industry.

Pepsin-Assisted Transglutaminase Modification of Functional Properties of a Protein Isolate Obtained from Industrial Sunflower Meal.

The utilization of industrial sunflower meal to produce protein-rich products for the food industry is an alternative approach for better and more efficient use of this agricultural by-product. Sunflower meal proteins possess specific functional properties, which however need improvement to broaden their potential as supplements for delivering high--quality products for human nutrition. The aim of the study is to evaluate the combined influence of low-degree pepsin hydrolysis and transglutaminase (TG) modification on industrial sunflower meal protein isolate functionality at pH=2 to 10. Three TG-modified pepsin hydrolysates with the degree of hydrolysis of 0.48, 0.71 and 1.72% were produced and named TG-PH1, TG-PH2 and TG-PH3, respectively. All three TG-modified pepsin hydrolysates exhibited improved solubility at pH between 3.5 and 5.5 as the highest was observed of TG-PH3 at protein isoelectric point (pI=4.5). Sunflower meal protein isolate and TG-modified sunflower meal protein isolate had greater solubility than the three TG-modified hydrolysates at pH<3 and >7. Significant improvement of foam making capacity (p<0.05) was achieved with all three TG-modified pepsin hydrolysates in the entire pH area studied. Pepsin hydrolysis of the protein isolate with the three degrees of hydrolysis did not improve foam stability. Improved thermal stability was observed with TG-PH3 up to 80 °C compared to the protein isolate (pH=7). At 90 °C, TG modification of the protein isolate alone resulted in the highest thermal stability. Pepsin hydrolysis followed by a treatment with TG could be used to produce sunflower protein isolates with improved solubility, foam making capacity and thermal stability for use in the food industry.