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HYPOTHESIS: Engineering plant-based microgel particles (MPs) at a molecular scale is meaningful to prepare functional fat analogues. We hypothesize that oat protein isolate (OPI) and κ-carrageenan (CA) have synergy in MPs formation, using MPs with controllable structure, and further to fabricate fat analogues with adjustable characteristics is feasible. Their digestion fate will also be possibly modulated by interfacial coatings. EXPERIMENTS: OPI-based conjugated MPs with tunable rigidities by changing crosslinking densities were designed. The relationship between microgel structures, and emulsion gel properties was explored through spectroscopy, microstructure, rheology and tribology. The delivery to lycopene, as well as inhibiting digestion behaviors of fat analogues was evaluated in a simulated gastro-intestinal tract. FINDINGS: The rigidity of conjugated MPs could be tailored to optimize the performance of fat analogues. OPI-1 %CA MPs could stabilize emulsions up to 95 % oil fraction with fine texture. Tribological behaviors had a dependence on microgel elasticity and interfacial coatings, medium hard MP-stabilized emulsion was less disrupted without coalescence after oral processing. Digestion was delayed by denser and harder MPs by softening the interfacial particle layer or limiting lipase accessibility. Softer conjugated MPs possessed better flexibility and were broken down more easily leading to a higher rate of lipid digestion.

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Oat protein isolate (OPI)/high methoxyl pectin (HMP) complexes (OPP) were prepared to stabilized Pickering emulsions and applied as nutraceutical delivery systems. The different mass ratios and pH changed the interactions between OPI and HMP that caused the different size of OPP. Specifically, smaller particle size of OPP (125.7-297.6 nm) were formed when hydrophobic interactions along with electrostatic forces predominant in OPP (OPI:HMP = 3:1, pH 4, 5). Among these particles, OPP-2 could stabilize Pickering emulsion efficiently through formation of dense interfacial film, which exhibited the highest apparent viscosity and the smallest average droplet size (23.39 µm). Moreover, OPP-2 stabilized Pickering emulsions with superior stability not only exhibited higher encapsulation efficiency of 85.63%, but also could control curcumin release in simulated gastrointestinal fluids to improve curcumin's bioaccessibility. These results verified the possibility of OPP to be a Pickering emulsions stabilizer, and also identified its potential to be a stable delivery system for bioactive compounds.

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The effect of genotype and environment on oat protein composition was analyzed through size exclusion-high-performance liquid chromatography (SE-HPLC) and liquid chromatography-mass spectrometry (LC-MS) to characterize oat protein isolate (OPI) extracted from three genotypes grown at three locations in the Canadian Prairies. SE-HPLC identified four fractions in OPI, including polymeric globulins, avenins, glutelins, and albumins, and smaller proteins. The protein composition was dependent on the environment, rather than the genotype. The proteins identified through LC-MS were grouped into eight categories, including globulins, prolamins/avenins, glutelins, enzymes/albumins, enzyme inhibitors, heat shock proteins, grain softness proteins, and allergenic proteins. Three main globulin protein types were also identified, including the P14812|SSG2-12S seed storage globulin, the Q6UJY8_TRITU-globulin, and the M7ZQM3_TRIUA-Globulin-1 S. Principal component analysis indicated that samples from Manitoba showed a positive association with the M7ZQM3_TRIUA-Globulin-1 S allele and Q6UJY8_TRITU-globulin, while samples from Alberta and Saskatchewan had a negative association with them. The results show that the influence of G × E on oat protein fractions and their relative composition is crucial to understanding genotypes' behavior in response to different environments.

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Oats are recognized to provide many health benefits that are mainly associated with its dietary fibre, ß-glucan. However, the protein derived from oats is largely understudied with respect to its ability to maintain health and attenuate risk factors of chronic diseases. The goal of the current study was to investigate the metabolic effects of oat protein consumption in lieu of casein as the protein source in high fat, high sucrose (HF/HS) fed Wistar rats. Four-week-old rats were divided into three groups and were fed three different experimental diets: a control diet with casein as the protein source, an HF/HS diet with casein, or an HF/HS diet with oat protein for 16 weeks. Heart structure and function were determined by echocardiography. Blood pressure measurements, an oral glucose tolerance test, and markers of cholesterol metabolism, oxidative stress, inflammation, and liver and kidney damage were also performed. Our study results show that incorporation of oat protein in the diet was effective in preserving systolic heart function in HF/HS fed rats. Oat protein significantly reduced serum total and low-density lipoprotein cholesterol levels. Furthermore, oat protein normalized liver HMG-CoAR activity, which, to our knowledge, is the first time this has been reported in the literature. Therefore, our research suggests that oat protein can provide hypocholesterolemic and cardioprotective benefits in a diet-induced model of metabolic syndrome.

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Oat protein is unstable in intestinal fluid digestion, and it is easily degraded by trypsin and chymotrypsin, producing low molecular weight peptides. Endopeptidase hydrolysis can improve the bioavailability of active peptides and avoid further digestion in the gastrointestinal tract. Antimicrobial peptides (AMPs) can effectively improve host immunity, but most related studies focus on physiology and ecology, and there are few reports on their molecular level. Therefore, in this article, oat peptides were prepared via the simulated digestion method in vitro, and the main metabolites and action factors affecting colitis were screened by using the multi-omics methods in a high-throughput mode to analyze the effect and mechanism of colitis. Firstly, oat antimicrobial peptides were prepared from cationic resin combined with HPLC, and the anti-inflammatory effects of antimicrobial peptides were analyzed in vitro through the use of human colon epithelial (HCoEpiC) anti-inflammatory cells. In vivo experiments using rats have verified that AMPs can effectively prevent colitis caused by dextran sodium sulfate (DSS), reduce intestinal inflammatory cell infiltration and glandular disappearance in the colon, and reduce the apoptosis rate of colon cells. Secondly, metabolomics and transcriptomics were combined to analyze the mechanism of preventing enteritis, and it was found that oat antimicrobial peptides can promote DAG diglycerol production and inhibit the activation of T helper cells (TH), resulting in the down-regulation of key factors in the main downstream pathways of TH1, TH2 and TH17, and inhibit the production of inflammatory cells. At the same time, AMP can activate the wnt pathway, improve the expression of key genes of wnt and frizzled, promote the generation of intestinal stem cells, facilitate the differentiation and repair of intestinal epithelial cells, and prevent the generation of enteritis. Finally, the underlying genetic regulatory network of the important pathway was constructed from the effect of AMP on rat colitis.

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Oat protein is becoming an important ingredient in beverages and formulated foods owing to its high nutritive value and bland flavor; yet, its functionality remains largely unexplored. This study sought to enhance the surface activity of oat protein isolate (OPI) through high-intensity ultrasound (HIU; at 20 or 60 °C) combined with high pressure homogenization (HP; 30 MPa) treatments. Sonication disturbed the protein conformation and significantly improved surface hydrophobicity (19.7%) and ζ-potential (15.7%), which were further augmented by subsequent HP (P < 0.05). Confocal microscopy revealed a uniform oil droplet distribution in emulsions prepared with HIU+HP combination treated OPI, and the oil droplet size decreased up to 35.6% when compared to that of non-treated OPI emulsion (d = 1718 nm). Emulsifying activity was greater for HIU+HP than for HIU, and the viscosity followed a similar trend. Moreover, while emulsions prepared with HIU or HP treated OPI were more stable than control, the 60 °C HIU+HP combination treatment yielded the maximum stability. In corroboration, a model salad dressing prepared from HIU+HP treated OPI displayed a homogenous oil droplet distribution and an improved viscosity. Therefore, thermosonication combined with high pressure homogenization may be suitable for salad dressings and other oil-imbedded food products.

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The heat treatment required for the deactivation of enzymes was carried out on crop species such as oats. Stir-frying, a frequently employed method for enzyme inactivation to preserve their desirable shelf life, can result in diminished nutritional value and protein degeneration. The mechanism by which stir-frying affects the oat protein remains largely unknown. Therefore, this study aimed to investigate the physicochemical and functional properties of the extracted oat protein isolates (OPI) at different stir-frying durations (0, 10, 20, and 30 min) at a temperature of 230 °C. The findings of this study demonstrated that stir-frying led to a decrease in the content of amino acids (AA), potentially attributed to the involvement of certain amino acids in the Maillard reaction. As the time of stir-frying increased, the secondary structure of OPI underwent changes: specifically, ß-turns transformed into ß-sheets. The process of protein denaturation and redistribution of chemical bonds resulted in an increase in the disulfide bond content of OPI, leading to aggregation, large particle size, and reduced digestibility. However, the water retention properties, foaming properties, and emulsification properties of OPI showed improvement. These findings provide valuable insights for the controlled and precise processing of oats and highlight the potential of OPI as a functional food.

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An oat protein concentrate (OC1) was isolated from oat flour through starch enzymatic hydrolysis, by subsequent defatting by ethanol and supercritical fluid extraction (SFE) reaching protein concentrations of 78% and 77% by weight in dry matter, respectively. The protein characterisation and functional properties of the defatted oat protein concentrates were evaluated, compared and discussed. The solubility of defatted oat protein was minor in all ranges of measured pH (3-9), and foamability reached up to 27%. Further, an oat protein concentrate defatted by ethanol (ODE1) was extruded by a single screw extruder. The obtained extrudate was evaluated by scanning electron microscope (SEM), texture and colour analysers. The extrudate's surface was well formed, smooth, and lacking a tendency to form a fibrillar structure. Textural analysis revealed a non-unform structure (fracturability 8.8-20.9 kg, hardness 26.3-44.1 kg) of the oat protein extrudate.

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The impact of novel pin-to-plate atmospheric cold plasma was investigated with input voltage (170 V, 230 V) and exposure time (15 & 30 min) on oat protein by studying structural (FTIR, circular dichroism (CD), UV-vis, Fluorescence), morphological (particle size analysis, SEM, turbidity), chemical (pH, redox potential (ORP), ζ potential, carbonyl, sulfhydryl, surface hydrophobicity), and foaming characteristics. The plasma treatment reduced the pH while increasing the ORP of the dispersions. These ionic environment changes affected the ζ potential and particle size leading to the formation of larger aggregates (170-15; 230-15) and distorted smaller ones (170-30; 230-30) as confirmed by SEM. The FTIR spectra showed reduced intensity at specific amide bands (1600-1700 cm-1) and also an increase in carbonyl stretching (1743 cm-1) representing oxidative carbonylation (increase in carbonyl content). Thus, the partial exposure of hydrophobic amino acids increases surface hydrophobicity. The altered secondary structure (rise in α-helix, decrement in ß-sheets and turns), and tertiary structures were observed in circular dichroism (CD) and UV absorbance and fluorescence characteristics of proteins respectively. Furthermore, the increase in free sulfhydryl content and disulfide content was highly affected by the plasma treatments due to observed protein unfolding and aggregations. Besides, the increased solubility and reduced surface tension contributed to the improved foaming characteristics. Thus, plasma processing influences protein structure affecting their characteristics and other functionalities.

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The aim of this study was to determine the effects of fermentation and food matrix on the ACE inhibitory activities of the peptides obtained after in vitro gastrointestinal digestion, protein profiles (SDS-PAGE) and ß-glucan amounts of oat products. Furthermore, the physicochemical and microbiological properties of fermented oat drinks and oat yogurt-like product obtained from oat fermentation were evaluated. Oat grains were mixed with a certain ratio of water 1:3 w/v (oat:water, yogurt consistency) and 1:5 w/v (oat:water, drink consistency), and this mixture was fermented with yogurt culture and probiotic Lactobacillus plantarum and fermented drinks and yogurt were produced. The results indicated that the fermented oat drink and the oat yogurt-like product had L. plantarum viability over 107 cfu/g. After the in vitro gastrointestinal digestion of the samples, the hydrolysis levels ranged from 57.70 % to 82.06 %.The hydrolysis level of the samples with fermented-drink consistency was significantly higher than the samples with yogurt consistency (p < 0.05).The SDS-PAGE profiles of the non-digested samples showed that the bands had molecular weights of 12-15 kDa and around 35 kDa. Bands whose molecular weights were around 35 kDA disappeared after gastric digestion. ACE inhibitory activities of the fractions composed of molecular weights of 2 kDa and 2-5 kDa obtained after in vitro gastrointestinal digestion of the oat samples were in the range of 46.93-65.91 %. The effect of fermentation on the ACE inhibitory activities of the peptide mixture with molecular weights between 2 and 5 kDa was not statistically significant, however, fermentation caused an increase in the ACE inhibitory activities of the peptide mixture with a molecular weight<2 kDa (p < 0.05). The ß-glucan amounts of fermented and non-fermented oat products were in the range of 0.57-1.28 %. The ß-glucan amounts detected after gastric digestion decreased considerably and ß-glucan could not be detected in the supernatant after gastrointestinal digestion. This indicated that ß-glucan did not solubilize in the supernatant (bioaccessible) and remained in the pellet. In conclusion, fermentation is a valuable process for releasing peptides with moderately high ACE inhibitory effects from the parent oat proteins.

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Oats are considered an exceptional source of high-quality protein. Protein isolation methods define their nutritional value and further applicability in food systems. The aim of this study was to recover the oat protein using a wet-fractioning method and investigate the protein functional properties and nutritional values among the processing streams. The oat protein was concentrated through enzymatic extraction, eliminating starch and non-starch polysaccharides (NSP), treating oat flakes with hydrolases, and reaching protein concentrations of up to about 86% in dry matter. The increased ionic strength from adding sodium chloride (NaCl) improved protein aggregation and resulted in increased protein recovery. Ionic changes improved protein recovery in provided methods by up to 24.8 % by weight. Amino acid (AA) profiles were determined in the obtained samples, and protein quality was compared with the required pattern of indispensable amino acids. Furthermore, functional properties of the oat protein, such as solubility, foamability, and liquid holding capacity, were investigated. The solubility of the oat protein was below 7 %; foamability averaged below 8%. The water and oil-holding reached a ratio of up to 3.0 and 2.1 for water and oil, respectively. Our findings suggest that oat protein could be a potential ingredient for food industries requiring a protein of high purity and nutritional value.

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Disulfide bonds play an essential structural role but may hinder the molecular flexibility and functionality of proteins. The present study investigated the effect of disulfide cleavage on emulsifying activity of oat protein isolate (OPI). Four reducing agents tested (dithiothreitol, ascorbic acid, cysteine, and sodium bisulfite) except ascorbic acid disrupted inter-subunit SS bonds of OPI (up to 90 %) in a dose-dependent manner. Emulsification properties were measured specifically on cysteine-modified OPI, and the results showed increased emulsifying activity up to 37 % after subunit dissociation, which exposed hydrophobic groups and loosened the structure. In particular, emulsions formed by cysteine-treated OPI (1.7 to 6.7 mM/mg protein) displayed a superior interfacial protein coverage (0.170 m2/mg compared to 0.092 m2/mg for control) and reduced emulsion particle size (from 4722 to 2238 nm). The application of cysteine as a structure-modifying food additive can broaden the utilization of oat protein in emulsion-based food products.

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This study developed two novel food packaging films, oat protein/pullulan (Op/Pul) and Nisin-loaded oat protein/pullulan (Nis@Op/Pul) films. Ultrasound was introduced to improve its mechanical, structural and physicochemical properties. The Op/Pul film has lower light transmittance, water vapour and oxygen permeability (OP) and improved film uniformity than pure oat protein and pullulan film. The addition of Nisin led to a significant decrease in the composite films' transparency, moisture content, and total soluble matter (TSM). The ultrasound treatment significantly increased the elongation at break and transparency of Nis@Op/Pul film by 18.37% and 8.03% and decreased its TSM and OP by 8.33% and 2.78%, respectively, compared to the conventional method. The structure analysis shows ultrasound enhances intermolecular hydrogen bonding, reduces the crystallinity and formed a more regular, uniform surface. Moreover, the Nis@Op/Pul film prepared by ultrasound treatment could effectively delay the decay and deterioration of fresh strawberries and prolong their shelf life.

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Oats are considered the healthiest grain due to their high content of phytochemicals, dietary fibers, and protein. In recent years, oat protein and peptides have gained popularity as possible therapeutic or nutraceutical candidates. Generally, oat peptides with bioactive properties can be obtained by the enzymatic hydrolysis of proteins and are known to have a variety of regulatory functions. This review article focused on the nutraceutical worth of oat proteins and peptides and also describes the application of oat protein as a functional ingredient. Outcomes of this study indicated that oat protein and peptides present various therapeutical properties, including antidiabetic, antioxidant, antihypoxic, antihypertensive, antithrombotic, antifatigue, immunomodulatory, and hypocholestrolaemic. However, most of the conducted studies are limited to in vitro conditions and less data is available on assessing the effectiveness of the oat peptides in vivo. Future efforts should be directed at performing systematic animal studies; in addition, clinical trials also need to be conducted to fully support the development of functional food products, nutraceutical, and therapeutical applications.

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The effect of enzyme treatment on protein-tannin interactions was investigated using up-to-date analytical approaches for improving their physical properties. The formation of ligands between procyanidin B2 and native oat globulin (OG) was observed to be affected by the ratio of procyanidin B2 to OG and the availability of tryptophan. For the transglutaminase-treated OG, the results obtained from circular dichroism (CD) and size exclusion chromatography (SEC) revealed that procyanidin B2 acted as an acyl acceptor in the process of OG deamidation. Procyanidin B2 also inhibited the non-covalent protein-protein interactions occurring between the aromatic side-chains or sedimentation of tryptophan aggregates. For trypsin-treated OG, procyanidin B2 interacted with phenylalanine and the tryptophan side-chain of OG. The inhibition of procyanidin B2 towards protein-protein aggregation was proved by the observation of CD, SEC and asymmetric flow field-flow fractionation.

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The aim of this study was to develop an extraction method to produce highly functional oat protein concentrates. We investigated the possibility of combining enzyme-aided slightly alkaline (pH 8.0) extraction with ultrafiltration and subsequent diafiltration for concentration of the extracted oat proteins. A further aim was to study how the deamidation of oat proteins with protein-glutaminase (PG) improves the solubility of proteins as a function of the following parameters: pH (6.0-9.0), enzyme dosage (4-20 U/g protein), and incubation time (1-4 h) with response surface methodology (RSM). Furthermore, we investigated selected functional properties, such as heat-induced gelation and solubility, of the oat protein concentrates. The chosen parameters for the enzymatic deamidation pre-treatment process by PG were as follows: pH 8.0, dosage 11.0 U/g protein, and an incubation time of 4 h (1 h at native pH and 3 h at pH 8.0). Two oat protein concentrates were produced, non-deamidated and ultrafiltered, and deamidated and ultrafiltered, with protein concentrations of 45.0 and 52.4%, respectively. The solubility of both oat protein concentrates was significantly improved at neutral and slightly alkaline pH compared to the solubility of proteins extracted from the starting material. Additionally, both oat protein concentrates produced equally strong heat-induced gel-like structures at a protein concentration of 10%.

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The consumer acceptance of alternative plant-focused ingredients within the meat industry is growing globally. Oat protein is insoluble and used to increase product yield and fat retention. Furthermore, inclusion of oat protein can provide manufacturers another option for extending beef supplies. As the consumer diet shifts for improvements in nutritional density, oat protein is an alternative ingredient that lacks information on inclusion in a ground beef formulation. Coarse ground beef was allocated to one of four treatments, mixed with oat protein (0%, 1.5%, 3.5% and 4.5%), water, salt, pepper, textured vegetable protein, soy protein concentrate, and sodium tripolyphosphate. Meat blocks (n = 3 batches) were finely ground and formed into patties (N = 65/treatment). Patties were placed onto an expanded polystyrene tray, overwrapped with polyvinyl chloride film and displayed for 7 days. Instrumental color (L*, a*, and b*) decreased throughout simulated display (p = 0.0001). Increased usage rates of oat protein in patties resulted in greater cook yields (p = 0.0001). Objective measures of Allo-Kramer shear force values increased as oat protein inclusion rates increased (p = 0.0001). Oat protein can be incorporated in ground beef patties with positive effects on cook yield, but inclusion rate may have a deleterious impact on color and instrumental tenderness.

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Blended meat/plant products are capturing industry market space at the retail counter for value-added beef products. Plant protein ingredients can be added to meat formulations to create appealing and functional products. Ground beef was combined with one of three plant protein inclusion treatments: control, pea, oat, or rice, along with 5% textured vegetable protein (TVP) and 1.5% soy protein concentrate then formed into 226 g patties containing up to 10% plant-based proteins. Patties were analyzed for fresh and cooked characteristics throughout a 5- or 7-day retail display. The inclusion of plant-based proteins negatively affected the instrumental tenderness values which were greater (p < 0.01) in plant-inclusion patties compared to the control patties. The inclusion of plant proteins increased (p = 0.01) the cooking yield of patties compared to the control. Cooking time was longer (p = 0.04) for oat patties compared to the control patties. Cooked color values for vegetable inclusion patties did not affect (p = 0.12) lightness (CIE L*) values; however, redness (CIE a*) was greater (p < 0.01) for rice than all other treatments and yellowness (CIE b*) values were greater (p < 0.01) for all protein treatments compared to the control. Rice improved (p < 0.01) fresh a* values on day 5 of display compared to the control; whereas pea decreased (p = 0.04) values compared to the control. There was a treatment × day interaction (p < 0.01) on lipid oxidation values with a reduction in values on day 3 for all vegetable proteins compared to the control and on day 7 lipid oxidation was reduced (p ≤ 0.03) for oat patties.

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Grain protein fractions have great potential as ingredients that contain high amounts of valuable nutritional components. The aim of this study was to study the rheological behavior of destarched oat and pea proteins and their blends in extrusion-like conditions with a closed cavity rheometer. Additionally, the possibility of producing fibrous structures with high-moisture extrusion from a blend of destarched oat and pea protein was investigated. In the temperature sweep measurement (60-160 °C) of the destarched oat protein concentrate and pea protein isolate blend, three denaturation and polymerization sections were observed. In addition, polymerization as a function of time was recorded in the time sweep measurements. The melting temperature of grain proteins was an important factor when producing texturized structures with a high-moisture extrusion. The formation of fibrillar structures was investigated with high-moisture extrusion from the destarched oat and pea protein blend at temperatures ranging from 140 to 170 °C. The protein-protein interactions were significantly influenced in the extruded samples. This was due to a decrease in the amount of extractable protein in selective buffers. In particular, there was a decrease in non-covalent and covalent bonds due to the formation of insoluble protein complexes.

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Understanding the relationship between ionic strength and protein solubility is essential to the utilization of salt in the formulation design of plant protein-based food and beverage products. In this study, suspensions of oat protein isolate (OPI) were treated with two kinds of common salts (sodium chloride NaCl; sodium phosphate NaP) at different ionic strengths (I). Electrical conductivity, protein solubility, particle size, and protein profile (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) were analyzed. The results showed the highest protein solubility at extremely low I (< 0.005 for NaCl; < 0.012 for NaP) and a minimum solubility at I 0.03 to 0.2 depending on the type of salt. Particle size and electrophoretic patterns supported the solubility profile. The combination effect of ionic strength and pH was also investigated. A characteristic U-shaped solubility curve observed within pH 2.0 to 8.0 at low ionic strengths (I < 0.01) was altered by increasing the salt concentration. The findings demonstrate that ionic strength and ion species play a crucial role in oat protein solubility, and the ionic effect can be modified by changing the pH. Therefore, the application of appropriate salt concentrations is vitally important to the manufacture of oat protein-based food products. PRACTICAL APPLICATION: Sodium chloride and phosphate are two of the most widely utilized salts in food processing. This study highlights the relationship between ionic strength of the two salts and oat protein solubility at different pH levels, providing useful information for selecting proper salt concentrations in the manufacture of oat protein-based food products.

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