RESUMO
Texturized Vegetable Protein (TVP), as meat analogs, has garnered attention due to the nutritional advantages it offers over conventional animal proteins. During the extrusion process of TVP, under the comprehensive effects of temperature, shear force, and pressure, complex conformational changes and molecular interactions amongst protein, carbohydrate, lipid, and other components occur, all of which influence the quality of TVP. Control of the extrusion process is still one of the largest challenges in its evolution. Therefore, this review aims to summarize the development and current status of food extrusion technology for TVP production and give detailed descriptions about the conformational changes of the main components during the extrusion process, focusing on the effects of barrel temperature, moisture content, feed rate and screw speed on TVP quality. Lastly, we discuss approaches to characterize the extrusion process and propose a new system analysis model.
Assuntos
Tecnologia de Alimentos , Proteínas de Vegetais Comestíveis/química , Alimentos de Soja , Pressão , Resistência ao Cisalhamento , TemperaturaRESUMO
Peanut allergy has garnered significant attention because of the high sensitization rate, increase in allergy, and severity of the reaction. Sufficiently reliable therapies and efficient mitigating techniques to combat peanut allergy are still lacking. Current management relies on avoiding peanuts and nuts and seeds with homologous proteins, although adverse events mostly occur with accidental ingestion. There is a need for hypoallergenic peanut products to protect sensitized individuals and perhaps serve as immunotherapeutic products. Alongside traditional practices of thermal and chemical treatment, novel processing approaches such as high-pressure processing, pulsed ultraviolet light, high-intensity ultrasound, irradiation, and pulsed electric field have been performed toward reducing the immunoreactivity of peanut. Covalent and noncovalent chemical modifications to proteins also have the tendency to alter peanut allergenicity. Enzymatic hydrolysis seems to be the most advantageous technique in diminishing the allergenic potential of peanut. Furthermore, the combined processing approach (hurdle technologies) such as enzymatic hydrolysis followed by, or in conjunction with, roasting, high pressure and heat, ultrasound with enzymatic treatment, or germination have shown a significant reduction of peanut immunoreactivity and may emerge as useful techniques in reducing the allergenicity of peanut and other foods. This study represents our current knowledge about the alterations in allergenic properties of peanut via different processing mechanisms as well as evaluating its future potential, geographical based data on increasing sensitization, clinical relevance, eliciting dose, and current management of peanut allergy. Furthermore, the molecular characteristics and clinical relevance of peanut allergens have been discussed.
RESUMO
In this study, the effect of different starches from corn, potato and pea containing varying amylose/amylopectin ratios on the textural and rehydration properties of extruded peanut protein gel particles were investigated. Results showed that textural and rehydration properties of peanut protein extruded with corn starch, potato starch and amylopectin are slightly inferior to those of peanut protein with pea starch extrudates. The addition of pea starch led to an increase in the pore structure of the peanut protein extrudates and improved their water absorption index, simultaneously reducing the hardness and density. Pea starch, as a natural water-absorbing expansion material, helped peanut protein to form cross-linked gel polymers that bind more water molecules, in addition to further polymerization with peanut protein, which made the protein secondary structure became disordered. These changes directly affected the textural properties of the extrudates. In addition, the blended system of starches and peanut protein tended to form more elastic solids, which affected the expansion of the extrudates. These findings indicate that starch can effectively improve the poor expansion of proteins, making it suitable for use in the production of plant protein-based foods.
RESUMO
In this study, the effects of different soluble proteins, including collagen peptides (CP), soy protein hydrolysate (HSPI), whey protein isolate (WPI), sodium caseinate (SC), and egg white protein (EWP), on the structural and mechanical properties of blends containing soy protein isolate (SPI) and wheat gluten (WG) were investigated using high-moisture extrusion. The addition of CP and HSPI resulted in a more pronounced fibrous structure with increased voids, attributing to their plasticizing effect that enhanced polymer chain mobility and reduced viscosity. WPI, SC, and EWP acted as crosslinking agents, causing early crosslink formation and decreased polymer chain mobility. These structural variations directly influenced the tensile properties of the extrudates, with CP displaying the highest anisotropic index. Moreover, the presence of soluble proteins impacts the permeability of the extrudates. These insights shed light on how soluble proteins can be used to modify the properties of SPI-WG blends, making them suitable for meat analogue production.
RESUMO
To provide a theoretical basis for the quality improvement of plant protein-based meat substitutes with lipids, the interactions between pea protein and fatty acids (stearic, oleic and linoleic acids) and the effect on protein conformational changes during high-moisture extrusion (HME) processing were investigated using a dead-stop operation. The surface hydrophobicity analysis and Fourier transform infrared spectroscopy results revealed that the fatty acids induced the exposure of hydrophobic groups in the pea proteins, weakened hydrogen bonds, affected the aggregation of legumin subunits and promoted the conversion of α-helix and ß-sheet structures to ß-turn and random coil during HME processing. In the die, unsaturated fatty acids limited the refolding of protein chains and covalent interactions between proteins. Micromorphology analysis indicated that the coalescence of oleic and linoleic acids in the cooling zone hindered the formation of anisotropic structures while stearic acid promoted the formation of fibrous structures by enhanced disulfide bonds.
Assuntos
Fabaceae , Proteínas de Ervilha , Ácidos Graxos/metabolismo , Ácidos Esteáricos/química , Ácidos Linoleicos , Fabaceae/metabolismo , Ligação de HidrogênioRESUMO
Low-moisture (20~40%) and high-moisture (40~80%) textured vegetable proteins (TVPs) can be used as important components of plant-based lean meat, while plant-based fat can be characterized by the formation of gels from polysaccharides, proteins, etc. In this study, three kinds of whole-cut plant-based pork (PBP) were prepared based on the mixed gel system, which were from low-moisture TVP, high-moisture TVP, and their mixtures. The comparisons of these products with commercially available plant-based pork (C-PBP1 and C-PBP2) and animal pork meat (APM) were studied in terms of appearance, taste, and nutritional qualities. Results showed the color changes of PBPs after frying were similar to that of APM. The addition of high-moisture TVP would significantly improve hardness (3751.96~7297.21 g), springiness (0.84~0.89%), and chewiness (3162.44~6466.94 g) while also reducing the viscosity (3.89~10.56 g) of products. It was found that the use of high-moisture TVP led to a significant increase in water-holding capacity (WHC) from 150.25% to 161.01% compared with low-moisture TVP; however, oil-holding capacity (OHC) was reduced from 166.34% to 164.79%. Moreover, essential amino acids (EAAs), the essential amino acids index (EAAI), and biological value (BV) were significantly increased from 272.68 mg/g, 105.52, and 103.32 to 362.65 mg/g, 141.34, and 142.36, respectively, though in vitro protein digestibility (IVPD) reduced from 51.67% to 43.68% due to the high-moisture TVP. Thus, the high-moisture TVP could help to improve the appearance, textural properties, WHC, and nutritional qualities of PBPs compared to animal meat, which was also better than low-moisture TVP. These findings should be useful for the application of TVP and gels in plant-based pork products to improve the taste and nutritional qualities.
RESUMO
Plant proteins can be extruded under high moisture content (above 40 %) to form meat-like fibrous structures, which is the basis for meat-like substitute products. However, the proteins' extrudability from various sources remain challenging in terms of generating fibrous structures under combinations of high-moisture extrusion with transglutaminase (TGase) modifications. In this study, proteins from soy (soy protein isolate, SPI, and soy protein concentrate, SPC), pea (pea protein isolate, PPI), peanut (peanut protein powder, PPP), wheat (wheat gluten, WG), and rice (rice protein isolate, RPI) were texturized using high-moisture extrusion combined with transglutaminase (TGase) modifications to enact changes in protein structure and extrusion capabilities. The results showed that soy proteins (SPI or SPC) responsed to torque, die pressure and temperature during extrusion, and this phenomenon was more pronounced at a higher protein content (SPI). In contrast, rice protein exhibited poor extrudability, leading to large losses of thermomechanical energy. TGase significantly affects the orientation of protein fibrous structures along the extrusion direction by impacting the rate of protein gelation during the high-moisture extrusion process, with the impact mainly occurring in the cooling die. Globulins (mainly 11S) played a major role in forming fibrous structures and the aggregation of globulins or reduction of gliadins under TGase modification impacted the orientation of the fibrous structure along the extrusion direction. Some thermomechanical treatment during high-moisture extrusion results in protein conversion from compact structure into more extended or stretched state, and the increase of random coil structures for proteins derived from wheat and rice would lead to these looser structures in the extrudates. Thus, TGase can be combined with high-moisture extrusion to regulate the formation of plant protein fibrous structures, dependent on the specific protein source and content.
Assuntos
Manipulação de Alimentos , Proteínas de Soja , Proteínas de Soja/química , Manipulação de Alimentos/métodos , Solubilidade , Transglutaminases/química , Glutens/química , Proteínas de Plantas/químicaRESUMO
To provide a deep insight into the application of lipid in plant protein-based meat substitutes through high-moisture extrusion (HME) process, the effect of fatty acid saturation degree (stearic acid, oleic acid and linoleic acid) on the rheological and structural properties of pea protein isolate (PPI), and its relationship with the extrusion system parameters and extrudate qualities were investigated. The oleic acid and linoleic acid significantly decreased the apparent viscosity of PPI dispersion and thus reduced the die pressure and torque during HME processing. Electrophoresis and Fourier transform infrared spectroscopy results revealed that fatty acids inhibited the aggregation of legumin and vicilin subunits at 50 and 20 kDa, and promoted the conversion of α-helix and ß-sheet to ß-turn and random coil. The macro- and micro-structure observation and texture analysis suggested that the fatty acids with higher unsaturation degree were not advantageous for the pea protein fibrous structure improvement during HME process.
Assuntos
Proteínas de Ervilha , Ácidos Graxos , Ácidos Linoleicos , Ácidos Oleicos , Reologia/métodosRESUMO
The high-moisture extrusion of proteins from plant and animal sources should be a new way for developing alternative protein products with meat-like texture. The protein gelling properties are considered an important factor for the meat-like texture formation during the high-moisture extrusion processing. In this study, the mixed protein gelling properties from soy protein isolate (SPI) and surimi at different ratios (90:10, 80:20, 70:30, 60:40 and 50:50) were investigated to relate to the high-moisture (70%) extruding product textural properties, correspondingly. Results showed that at SPI-surimi ratio 60:40, the heat-induced gelation time was clearly extended and the gel strength became much weaker. During the high-moisture extrusion processing, at SPI-surimi ratio 80:20, the extrudate showed the higher hardness, chewiness, gel strength and fibrous degree, while excessive surimi (more than 40%) in the blends would hinder the fibrous-oriented structure formation. It suggested that SPI may act as the continuous phase that is dispersed by surimi during the high-moisture extrusion processing. Interestingly, it was found that the gel strength of SPI-surimi blends was nonlinearly correlated with the specific mechanical energy (SME) and product textural properties. The study would be helpful for improving the textural properties of alternative protein products from soy and surimi.
RESUMO
The effect of high-moisture extrusion (HME) with or without transglutaminase (TGase) on peanut allergen levels and their extractability was studied. A three-stage sequential protein extraction significantly improved the protein recovery in processed samples (extrudate meat analogue); from 5.56 to 18.75 mg/100 mg without TGase, and from 4.59 to 20.82 mg/100 mg with 0.3% TGase. The total major allergen content was reduced by 91% (Ara h 1), 61% (Ara h 2), 60% (Ara h 6), and 55% (Ara h 3). Western-blot analysis of soluble extracts reflected the presence of Ara h 1 and Ara h 2 in significantly lower, indicating a potential reduction in IgE binding. During different processing zones, the most significant reduction in allergenic proteins was in the melting zone. The significant alteration in secondary and tertiary structures as a result of crosslinking shearing and degradation of proteins is likely to lead to allergen reduction.
Assuntos
Arachis , Hipersensibilidade a Amendoim , Alérgenos/química , Antígenos de Plantas/química , Arachis/química , Imunoglobulina E/metabolismo , Proteínas de Plantas/metabolismo , TransglutaminasesRESUMO
In meat processing, changes in the myofibrillar protein (MP) structure can affect the quality of meat products. High hydrostatic pressure (HHP) has been widely utilized to change the conformational structure (secondary, tertiary and quaternary structure) of MP so as to improve the quality of meat products. However, a systematic summary of the relationship between the conformational structure (secondary and tertiary structure) changes in MP, gel properties and product quality under HHP is lacking. Hence, this review provides a comprehensive summary of the changes in the conformational structure and gel properties of MP under HHP and discusses the mechanism based on previous studies and recent progress. The relationship between the spatial structure of MP and meat texture under HHP is also explored. Finally, we discuss considerations regarding ways to make HHP an effective strategy in future meat manufacturing.
RESUMO
Converting peanut protein biomass waste into environmentally friendly meat substitutes by a high-moisture extrusion process can help solve both resource and waste problems and be "double green". A multiscale method combined with some emerging techniques such as atomic force microscopy-based infrared spectroscopy and X-ray microscopy was used to make the whole extrusion process visible to show the process of forming a meat-like fibrous structure using two-dimensional and three-dimensional perspectives. The results showed that the protein molecules underwent dramatic structural changes and unfolded in the extruder barrel, which created favorable conditions for molecular rearrangement in the subsequent zones. It was confirmed that the meat-like fibrous structure started to form at the junction of the die and the cooling zone and that this structure was caused by the phase separation and rearrangement of protein molecules in the cooling zone. Moreover, the interactions between hydrogen bonds and disulfide bonds formed in the cooling zone maintained the meat-like fibrous structure with an α-helix > ß-sheet > ß-turn > random coil. Of the two main peanut proteins, arachin played a greater role in forming the fibrous structure than conarachin, especially those subunits of arachin with a molecular weight of 42, 39, and 22 kDa.