Insight into the mechanism of the aggregation behavior of wheat protein modulated by l-lysine under microwave irradiation.

This study explored the mechanism of l-lysine intervention in wheat gluten protein (WG) gel formation under a microwave (MW) field. The results showed that the MW treatment had higher ζ-potential values at the same heating rate. After adding l-lysine, the solution conductivity and dielectric loss were significantly increased. Moreover, the WG gel strength enhanced 4.40% under the MW treatment. The Fourier spectra showed that the α-helix content was decreased 13.78% with the addition of lysine. The ultraviolet absorption spectra and fluorescence spectra indicated that MW irradiation impacted the interactions between WG molecules more effectively than the water bath heating, promoting the denaturation and unfolding of the protein structure. In addition, scanning electron microscopy analysis showed that the incorporation of lysine promoted an ordered network structure formation of the protein, which enhanced the gel properties. This indicated that the zwitterion of l-lysine played a regulatory role in the aggregation of proteins in the MW field.

The flavour of wheat gluten hydrolysate after Corynebacterium Glutamicum fermentation: Effect of degrees of hydrolysis and fermentation time.

Corynebacterium glutamicum was used to ferment wheat gluten hydrolysates (WGHs) to prepare flavour base. This study investigated the effect of hydrolysis degrees (DHs) and fermentation time on flavour of WGHs. During fermentation, the contents of amino nitrogen, total acid and small peptides increased, while the protein and pH value decreased. Succinic acid, GMP, and Glu were the prominent umami substances in fermented WGHs. The aromas of WGHs with different DHs could be distinguished by electronic nose and GC-IMS. Based on OAV of GC-MS, hexanal was the main compound in WGHs, while phenylethyl alcohol and acetoin were dominant after fermentation. WGHs with high DHs accumulated more flavour metabolites. Correlation analysis showed that small peptides (<1 kDa) could promote the formation of flavour substances, and Asp was potentially relevant flavour precursor. This study indicated that fermented WGHs with different DHs can potentially be used in different food applications based on flavour profiles.

Molecular docking and molecular dynamics simulation of wheat gluten-derived antioxidant peptides acting through the Keap1-Nrf2 pathway.

BACKGROUND: In our previous study, we successfully identified five peptides from wheat gluten: Ala-Pro-Ser-Tyr (APSY), Leu-Tyr (LY), Pro-Tyr (PY), Arg-Gly-Gly-Tyr (RGGY) and Tyr-Gln (YQ). Molecular docking and molecular dynamics simulation methods were employed to investigate the interaction between these antioxidant peptides and the Kelch-like ECH-associated protein 1 (Keap1 protein), revealing the molecular mechanism of their non-competitive binding. In addition, the total antioxidant capacity of the five peptides was determined using the 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) method. RESULTS: The affinities of APSY, LY, PY, RGGY and YQ were -8.9, -8.3, -8.5, -9.1 and - 7.9 kcal mol-1, respectively. The five peptides effectively bound to Keap1 protein through hydrogen, π-σ, π-alkyl and alkyl interactions. Significant roles were observed for the P1 pocket residue ARG-415 and the P3 pocket residue ALA-556 in the interactions of the Keap1-peptide complexes. Molecular dynamics simulations further elucidated the dynamic process of peptide binding to the Keap1 protein. All five peptides formed stable complexes with Keap1 protein, with van der Waals forces playing crucial roles in these complex systems, indicative of the peptides' strong binding ability to Keap1 protein. The van der Waals forces were -178.74, -123.11, -134.36, -132.59, and -121.44 kJ mol-1 for the Keap1-APSY, Keap1-LY, Keap1-PY, Keap1-RGGY and Keap1-YQ complexes, respectively. These peptides exhibited excellent antioxidant effects. Among them, the YQ peptide exhibited the highest total antioxidant capacity, with an activity value of 1.18 ± 0.06 mmol Trolox equivalent (TE) L-1 at a concentration of 0.10 mg mL-1. The RGGY, PY, LY and APSY peptides followed in descending order, with activity values of 0.91 ± 0.05, 0.72 ± 0.06, 0.62 ± 0.04 and 0.60 ± 0.05 mmol TE L-1, respectively. CONCLUSION: These results unveiled the molecular mechanism by which the five antioxidant peptides act on active pockets through the Keap1-Nrf2 signaling pathway, providing a theoretical basis for the development of antioxidants. © 2024 Society of Chemical Industry.

Effects of different polysaccharide colloids on the structure and physicochemical properties of peanut protein and wheat gluten composite system under extrusion.

The structure and physicochemical properties of the complex system of peanut protein and gluten with different concentrations (0 %, 0.5 %, 1 %, and 2 %) of carboxymethyl cellulose (CMC) or sodium alginate (SA) under high-moisture extrusion were studied. The water absorption index and low-field nuclear magnetic resonance showed that adding 0.5 % SA could significantly improve the water uniformity of peanut protein extrudates, while the increase in water absorption was not significant. The texture properties showed that adding CMC or SA increased the hardness, vertical shearing force, and parallel shearing force of the system. Furthermore, adding 0.5 % SA increased approximately 33 % and 75.2 % of the tensile distance and strength of the system, respectively. The secondary structure showed that CMC or SA decreased the proportion of α-helix, ß-turn, and random coil, while increased ß-sheet proportion. The results of hydrophobicity, unextractable protein, and endogenous fluorescence revealed that CMC and SA reduced the surface hydrophobicity of the system and caused fluorescence quenching in the system. Additionally, it was found that CMC generally increased the free sulfhydryl group content, while SA exhibited the opposite effect.

Development of environmentally friendly glyoxal-based adhesives with outstanding water repellency utilizing wheat gluten protein.

To reduce the release of volatile organic compounds (VOCs) from formaldehyde-based adhesives at the source, the use of low-toxicity and biodegradable glyoxal instead of formaldehyde for the preparation of novel urea-glyoxal resins is a simple and promising strategy. The limited water resistance and adhesive strength of the new urea-glyoxal resins (UG) restrict their extensive application. This study prepared a high-performance, water-resistant WP-UG wood adhesive by combining UG prepolymer with wheat gluten protein (WP). FTIR, XRD, and XPS confirmed the existence of a chemical reaction between the two components, and thermal analysis showed that WP-UG plywood had better thermal stability. Evaluation of the gluing properties revealed that the dry and wet strengths of WP-UG adhesive bonded plywood reached 1.39 and 0.87 MPa, respectively, which were significantly higher than those of UG resin by 35 % and 314 %. The bond strength increased from 0 to 0.89 MPa after immersion in water at 63 °C for 3 h. The results indicated that the introduction of WP promoted the formation of a more complex and tightly packed crosslinking network and developed a glyoxal-based adhesive with high bond strength and water resistance. This study provides a new green pathway for novel urea-formaldehyde binders to replace harmful formaldehyde-based binders, which helps to increase their potential application value in the wood industry.

Wheat gluten structure and (non-)covalent network formation during deep-fat frying.

The aim of this work was to investigate wheat gluten protein network structure throughout the deep-frying process and evaluate its contribution to frying-induced micro- and macrostructure development. Gluten polymerization, gluten-water interactions, and molecular mobility were assessed as a function of the deep-frying time (0 - 180 s) for gluten-water model systems of differing hydration levels (40 - 60 % moisture content). Results showed that gluten protein extractability decreased considerably upon deep frying (5 s) mainly due to glutenin polymerization by disulfide covalent cross-linking. Stronger gliadin and glutenin protein-protein interactions were attributed to the formation of covalent linkages and evaporation of water interacting with protein chains. Longer deep-frying (> 60 s) resulted in progressively lower protein extractabilities, mainly due to the loss in gliadin protein extractability, which was associated with gliadin co-polymerization with glutenin by thiol-disulfide exchange reactions. The mobility of gluten polymers was substantially reduced during deep-frying (based on the lower T2 relaxation time of the proton fraction representing the non-exchanging protons of gluten) and gluten proteins gradually transitioned from the rubbery to the glassy state (based on the increased area of said protons). The sample volume during deep-frying was strongly correlated to the reduced protein extractability (r = -0.792, p < 0.001) and T2 relaxation time of non-exchanging protons of gluten proteins (r = -0.866, p < 0.001) thus demonstrating that the extent of gluten structural expansion as a result of deep-frying is dictated both by the polymerization of proteins and the reduction in their molecular mobility.

Amyloid-like Aggregation of Wheat Gluten and Its Components during Cooking: Mechanisms and Structural Characterization.

Amyloid-like aggregation widely occurs during the processing and production of natural proteins, with evidence indicating its presence following the thermal processing of wheat gluten. However, significant gaps remain in understanding the underlying fibrillation mechanisms and structural polymorphisms. In this study, the amyloid-like aggregation behavior of wheat gluten and its components (glutenin and gliadin) during cooking was systematically analyzed through physicochemical assessment and structural characterization. The presence of amyloid-like fibrils (AFs) was confirmed using X-ray diffraction and Congo red staining, while Thioflavin T fluorescence revealed different patterns and rates of AFs growth among wheat gluten, glutenin, and gliadin. AFs in gliadin exhibited linear growth curves, while those in gluten and glutenin showed S-shaped curves, with the shortest lag phase and fastest growth rate (t1/2 = 2.11 min) observed in glutenin. Molecular weight analyses revealed AFs primarily in the 10-15 kDa range, shifting to higher weights over time. Glutenin-derived AFs had the smallest ζ-potential value (-19.5 mV) and the most significant size increase post cooking (approximately 400 nm). AFs in gluten involve interchain reorganization, hydrophobic interactions, and conformational transitions, leading to additional cross ß-sheets. Atomic force microscopy depicted varying fibril structures during cooking, notably longer, taller, and stiffer AFs from glutenin.

Data on antimicrobial, barrier, and mechanical properties of biocomposites prepared from carrot pomace and wheat gluten with varied eugenol content.

This article presents analyzed data on the antimicrobial, barrier, and mechanical properties inherent to films created by blending carrot pomace with wheat gluten and polyglycerol-3 plasticizer and combined with varying contents (0 wt.%, 3 wt.%, and 5 wt.%) of eugenol, a natural antimicrobial compound derived from essential oils. The integration of carrot pomace, wheat gluten, plasticizer, and eugenol involved meticulous mortar and pestle processing, ensuring a homogenous blend. Subsequently, the mixture was compression-molded in a hydraulic press to fabricate the films. Standard bacteria strains-Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 6538-are used in the antimicrobial evaluation, and antimicrobial efficacy is measured using OD600 measurements. Water vapor permeability (WVP) measurement effectively defines the films' potential to prevent water vapor infiltration. Mechanical properties are assessed by determining elastic modulus, tensile strength, and elongation at break, which together reveal the films' adaptive flexibility and durability. The dataset presented herein holds substantial promise for food packaging applications. Researchers in the food packaging industry can leverage the antimicrobial and barrier property data to design novel packaging materials, potentially enhancing shelf-life and food safety. Engineers and material scientists can utilize the mechanical properties data to develop structurally robust and flexible materials.

Blueberry anthocyanin based active intelligent wheat gluten protein films: Preparation, characterization, and applications for shrimp freshness monitoring.

The aim of this study was to prepare active intelligent gluten protein films using wheat gluten protein (WG) and apple pectin (AP) as film-forming matrices, and blueberry anthocyanin extract (BAE) as a natural indicator. SEM and FT-IR analyses demonstrated the successful immobilization of BAE in the film matrix by hydrogen bonding interactions and its compatibility with WG and AP. The resultant WG-AP/BAE indicator films demonstrated notable antioxidant activity, color stability, barrier qualities, pH and ammonia response sensitivity, and mechanical properties. Among them, WG-AP/BAE5 exhibited the best mechanical properties (TS: 0.83 MPa and EB: 242.23%) as well as the lowest WVP (3.92 × 10-8 g.m/m2.Pa.s), and displayed high sensitivity to volatile ammonia. In addition, WG-AP/BAE5 showed a color shift from purplish red to green to yellowish green, demonstrating the monitoring of shrimp freshness in real time. Consequently, this study offers a firm scientific foundation for the development of active intelligent gluten protein films and their use in food freshness assessments.

Synergistic impact of heat and salicylic acid pretreatment on gluten films: Characterization and functional properties.

This study investigates how wheat gluten (WG) films in the presence of salicylic acid are influenced by thermal pretreatment. Unlike previous methods conducted at low moisture content, our procedure involves pretreating WG at different temperatures (65 °C, 75 °C, and 85 °C), in a solution with salicylic acid. This pretreatment aims to enhance protein unfolding, thus providing more opportunities for protein-protein interactions during the subsequent solvent casting into films. A significant increase in ß-sheet structures was observed in FTIR spectra of samples pretreated at 75 °C and 85 °C, showing a prominent peak in the range of 1630-1640 cm-1. The pretreatment at 85 °C was found to be effective in improving the water resistivity of the films by up to 247 %. Moreover, it led to a significant enhancement of 151 % in tensile strength and a 45 % increase in the elastic modulus. The reduced solubility observed in films derived from pretreated WG suggests the development of an intricate protein network arising from protein-protein interactions during the pretreatment and film formation. Thermal pretreatment at 85 °C significantly enhances the structural and mechanical properties of WG films, including improved water resistivity, tensile strength, and intricate protein network formation.

Purified protein glutaminase from Chryseobacterium proteolyticum enhances the properties of wheat gluten.

Protein glutaminase (PG), originating from Chryseobacterium proteolyticum, can catalyze the deamidation of glutamine residues in plant proteins into glutamic acid, thus enhancing its functional properties. However, the low yield of PG limits its industrial production. In this study, the yield of PG in C. proteolyticum TM1040 increased by 121 %, up to 7.30 U/mL in a 15 L fermenter after medium optimization. Subsequently, purified PG was obtained by cation exchange chromatography (CEX) coupled with hydrophobic interaction chromatography (HIC). The degree of deamidation (DD) of wheat gluten after purified PG deamidation was 87.11 %, which is superior to chemical deamidation in safety and DD. The emulsifying and foaming properties of deamidated wheat gluten were 2.67 and 18.86 times higher, and the water- and oil-holding properties were 4.23 and 18.77 times higher, respectively. The deamidated wheat gluten with enhanced functional properties was used to improve the flavor and texture in baking cakes.

Insight into the solubilization mechanism of wheat gluten by protease modification from conformational change and molecular interaction perspective.

The low solubility limits the utilization of other functional characteristics of wheat gluten (WG). This study effectively improved the solubility of WG through protease modification and explored the potential mechanism of protease modification to enhance the solubility of WG, further stimulating the potential application of WG in the food industry. Solubility of WG modified with alkaline protease, complex protease, and neutral protease was enhanced by 98.99%, 54.59%, and 51.68%, respectively. Notably, the content of ß-sheet was reduced while the combined effect of hydrogen bond and ionic bond were increased after protease modification. Meanwhile, the reduced molecular size and viscoelasticity as well as the elevated surface hydrophobicity, thermostability, water absorption capacity, and crystallinity were observed in modified WG. Moreover, molecular docking indicated that protease was specifically bound to the amino acid residues of WG through hydrogen bonding, hydrophobic interaction, and salt bridge.

Effect of ficin-hydrolyzed wheat gluten on bread quality and in vitro antioxidant activity before and after simulated gastrointestinal digestion.

This study aimed to investigate the effect of adding ficin-hydrolyzed wheat gluten at different levels (0%, 1%, 2%, 4%) on bread quality, and in vitro antioxidant activity before and after simulated gastrointestinal digestion. Our findings revealed that the incorporation of the generated wheat gluten hydrolysates (WGH) up to 4 g per 100 g flour positively affected the technological and physical-chemical characterizations of breads, including dough rheological properties, color, specific volume, and moisture. The texture profile analysis indicated reductions in hardness, springiness, and chewiness of the breads, and confirmed anti-staling properties during storage. The enriched breads received satisfactory scores from the sensory panel and were perceived as less stale after a 4-day period of storage. The aroma score of the 4% WGH bread was significantly higher than other treatments. Regarding taste, the 4% WGH bread scored the lowest, but the obtained value was not statistically significant. The enriched breads exhibited DPPH, ABTS radical scavenging, and Fe2+ chelation abilities that increased in response to higher levels of hydrolysate incorporation, and these antioxidant activities were enhanced after simulated gastrointestinal digestion. Our findings confirm that it is possible to apply ficin-generated WGH to enhance physicochemical, nutritional, and biological quality of bread.

High Fischer Ratio Oligopeptides of Gluten Alleviate Alcohol-Induced Liver Damage by Regulating Lipid Metabolism and Oxidative Stress in Rats.

High Fischer ratio oligopeptides (HFOs) exhibit diverse biological activities, including anti-inflammatory and antioxidant properties. HFOs from gluten origin were prepared through fermentation and enzymatic hydrolysis and then characterized using free amino acid analysis and scanning electron microscopy (SEM). Following intervention, the levels of serum total cholesterol (TC), triglyceride (TG), alanine aminotransferase (ALT), aspartate aminotransferase (AST), and hepatic malondialdehyde (MDA) in the rats significantly decreased (p < 0.05). Simultaneously, there was an increasing trend in superoxide dismutase (SOD) levels, and glutathione (GSH) levels were significantly elevated (p < 0.05). The mRNA expression levels of alcohol metabolism-related genes (ADH4, ALDH2, and CYP2E1) exhibited a significant increase (p < 0.05). Histological examination revealed a reduction in liver damage. The findings indicate that high Fischer ratio oligopeptides, prepared through enzymatic and fermentation methods, significantly improve lipid levels, ameliorate lipid metabolism disorders, and mitigate oxidative stress, and exhibit a discernible alleviating effect on alcoholic liver injury in rats.

Wheat gluten deamidation: structure, allergenicity and its application in hypoallergenic noodles.

BACKGROUND: Wheat gluten (WG) containing gliadin and glutenin are considered the main allergens in wheat allergy as a result of their glutamine-rich peptides. Deamidation is a viable and efficient approach for protein modifications converting glutamine into glutamic acid, which may have the potential for allergenicity reduction of WG. RESULTS: Deamidation by citric acid was performed to investigate the effects on structure, allergenicity and noodle textural properties of wheat gluten (WG). WG was heated at 100 °C in 1 m citric acid to yield deamidated WG with degrees of deamidation (DD) ranging from DWG-25 (25% DD) to DWG-70 (70% DD). Fourier-transform infrared and intrinsic fluorescence spectroscopy results suggested the unfolding of WG structure during deamidation, and sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed molecular weight shifts at the 35-63 kDa region, suggesting that the deamidation mainly occurred on low molecular weight glutenin subunits and γ- gliadin of the WG. An enzyme-linked immunosorbent assay of deamidated WG revealed a decrease in absorbance and immunoblotting indicated that the intensities of protein bands at 35-63 kDa decreased, which suggested that deamidation of WG might have caused a greater loss of epitopes than the generation of new epitopes caused by unfolding of WG, and thereby reduction of the immunodominant immunoglobulin E binding capacity, ultimately leading to the decrease in allergenicity. DWG-25 was used in the preparation of recombinant hypoallergenic noodles, and the hardness, elasticity, chewiness and gumminess were improved significantly by the addition of azodicarbonamide. CONCLUSION: The present shows the potential for deamidation of the WG products used in novel hypoallergenic food development. © 2023 Society of Chemical Industry.

A multiple cross-linking strategy to develop an environment-friendly and water resistance wheat gluten protein wood adhesive.

Wheat gluten (WG) shows great promise to synthesize environment-friendly wood adhesives. However, their weak bonding strength and poor water resistance have limited its application in the commercial wood-based panel industry. In this study, a novel WG-based adhesive was developed by constructing a multiple cross-linking network generated by covalent and non-covalent bonds. The potential mechanism was revealed by FT-IR analysis. Furthermore, their surface morphology, thermal stability, viscosity, and residual rate of adhesives with different compositions were systematically characterized and compared. The results showed that the hydrogen bonding, reactions between amine groups and tannin, and ring opening reaction of epoxy, synergistically contributed to generate a highly crosslinked network. The wet/boil water strength of the plywood prepared from WG/tannin/ethylene imine polymer (PEI)-glycerol triglycidyl ether (GTE) adhesive with the addition of 15 % GTE could reach 1.21 MPa and 1.20 MPa, respectively, and a mildew resistance ability was observed. This study provides a facile strategy to fabricate high-performance plant protein-based adhesives with desirable water resistance for practical application.

Evaluation of different Starch Binders on physical quality of fish feed pellets / Avaliação de diferentes aglutinantes de amido na qualidade física de rações para peixes

Binders are the products that are used to bind, glue or hold the various feed ingredients together in order to maintain pellet integrity. For aqua-culturists, feed manufacturing is an expensive exercise due to the high cost of ingredients along with traditional artificial binders. The use of grain starches as aqua feed binders have advantages which include availability of that binder, nutritional contribution, and minimization of feed cost. A research trial was conducted to test physical properties such as palatability, water stability, dustiness, friability, settling velocity and floatation time of locally available starch i.e. wheat gluten, pea starch and guar gum and to assist their incorporation in on-farm aqua feed. Results revealed that among these three starch, the starch from pea source was proved superior over other two (wheat gluten and guar gum) as all physical quality parameters (dustiness, water stability and friability) revealed better performance of pea starch except pelletability in which guar gum performed best. Although not a single diet proved best in case of flotation time (Tf) and settling velocity (Vset) at varying lengths (6mm, 9mm and 12 mm). This finding indicates the significance of suitable binders for optimal water pollution and sustainable aquaculture. The use of these binders i.e. wheat gluten, pea starch and guar gum in fish feed pellets may also reduce dependence on synthetic binders and minimizes cost.

Aglutinantes são produtos usados para unir, colar ou manter juntos os vários ingredientes da ração, a fim de conservar a integridade do pellet. Para os aquicultores, a fabricação de ração é uma atividade difícil e cara por causa do alto preço dos aglutinantes artificiais tradicionais. O uso de amidos de grãos como aglutinantes de rações aquáticas tem vantagens que incluem acessibilidade, disponibilidade, contribuição nutricional e minimização do custo da ração. Um ensaio de pesquisa foi conduzido para testar propriedades físicas, como palatabilidade, estabilidade em água, pulverulência, friabilidade, velocidade de sedimentação e tempo de flutuação de amido disponível localmente, ou seja, glúten de trigo, amido de ervilha e goma de guar, e para auxiliar sua incorporação em rações aquáticas. Os resultados revelaram que, entre esses três amidos, o amido de ervilha se mostrou superior aos outros dois (glúten de trigo e goma de guar), pois todos os parâmetros de qualidade física (pulverulência, estabilidade da água e friabilidade) obtiveram melhor desempenho, exceto peletabilidade, em que a goma de guar se destacou. Nenhuma dieta se mostrou melhor no caso de tempo de flotação (Tf) e velocidade de sedimentação em comprimentos variados (6 mm, 9 mm e 12 mm). Essa descoberta indica a importância de aglutinantes adequados para a poluição ótima da água e a aquicultura sustentável. O uso desses aglutinantes, ou seja, glúten de trigo, amido de ervilha e goma de guar, em pellets de ração para peixes também pode reduzir a dependência de aglutinantes sintéticos e minimizar o custo.

Evaluation of different Starch Binders on physical quality of fish feed pellets

Abstract Binders are the products that are used to bind, glue or hold the various feed ingredients together in order to maintain pellet integrity. For aqua-culturists, feed manufacturing is an expensive exercise due to the high cost of ingredients along with traditional artificial binders. The use of grain starches as aqua feed binders have advantages which include availability of that binder, nutritional contribution, and minimization of feed cost. A research trial was conducted to test physical properties such as palatability, water stability, dustiness, friability, settling velocity and floatation time of locally available starch i.e. wheat gluten, pea starch and guar gum and to assist their incorporation in on-farm aqua feed. Results revealed that among these three starch, the starch from pea source was proved superior over other two (wheat gluten and guar gum) as all physical quality parameters (dustiness, water stability and friability) revealed better performance of pea starch except pelletability in which guar gum performed best. Although not a single diet proved best in case of flotation time (Tf) and settling velocity (Vset) at varying lengths (6mm, 9mm and 12 mm). This finding indicates the significance of suitable binders for optimal water pollution and sustainable aquaculture. The use of these binders i.e. wheat gluten, pea starch and guar gum in fish feed pellets may also reduce dependence on synthetic binders and minimizes cost.

Resumo Aglutinantes são produtos usados para unir, colar ou manter juntos os vários ingredientes da ração, a fim de conservar a integridade do pellet. Para os aquicultores, a fabricação de ração é uma atividade difícil e cara por causa do alto preço dos aglutinantes artificiais tradicionais. O uso de amidos de grãos como aglutinantes de rações aquáticas tem vantagens que incluem acessibilidade, disponibilidade, contribuição nutricional e minimização do custo da ração. Um ensaio de pesquisa foi conduzido para testar propriedades físicas, como palatabilidade, estabilidade em água, pulverulência, friabilidade, velocidade de sedimentação e tempo de flutuação de amido disponível localmente, ou seja, glúten de trigo, amido de ervilha e goma de guar, e para auxiliar sua incorporação em rações aquáticas. Os resultados revelaram que, entre esses três amidos, o amido de ervilha se mostrou superior aos outros dois (glúten de trigo e goma de guar), pois todos os parâmetros de qualidade física (pulverulência, estabilidade da água e friabilidade) obtiveram melhor desempenho, exceto peletabilidade, em que a goma de guar se destacou. Nenhuma dieta se mostrou melhor no caso de tempo de flotação (Tf) e velocidade de sedimentação em comprimentos variados (6 mm, 9 mm e 12 mm). Essa descoberta indica a importância de aglutinantes adequados para a poluição ótima da água e a aquicultura sustentável. O uso desses aglutinantes, ou seja, glúten de trigo, amido de ervilha e goma de guar, em pellets de ração para peixes também pode reduzir a dependência de aglutinantes sintéticos e minimizar o custo.

Effect of l-cysteine on functional properties and fibrous structure formation of 3D-printed meat analogs from plant-based proteins.

The development of three-dimensional (3D) printed meat analogs with fiber, texture, and sensory resembling meat remains challenging. This study investigated the effect of l-cysteine on functionality enhancement and fibrous structure formation in mixtures of mung bean protein isolate (MBPI) and wheat gluten (WG) for meat analog production. 3D printing was used to construct fibrous filaments. Raw MBPI-WG mixtures decreased rheological properties when increasing l-cysteine contents (0.0%-0.6%), promoting ink extrudability. The cys-0.4% ink exhibited the highest printing resolution and structural stability, correlated with its higher mechanical strength and increased disulfide cross-links. After cooking, the cys-0.4% sample showed a pronounced fibrousness in agreement with its microstructure image. This meat analog displayed a muscle-meat-like structure, improved texture, and reduced beany odor and bitter taste. Excessive cysteine contents (0.5%-0.6%) negatively affected the functionality of meat analogs. This study provides guidance for optimizing the amount of l-cysteine in meat analogs to improve product quality.

Effect of insoluble dietary fiber on printing properties and molecular interactions of 3D-printed soy protein isolate-wheat gluten plant-based meats.

Insoluble dietary fiber (IDF) has been characterized to prevent chronic diseases and improve gastrointestinal health, and it has been added to 3D printing plant-based meats (PM) to enhance texture and increase nutritional properties. Therefore, the aim of this study was to investigate the effects of IDF on 3D printing properties and molecular interactions of soy protein isolate (SPI) - wheat gluten (WG) PM. Without the participation of IDF, PM appeared to collapse. When the IDF concentration increased from 0 to 10 %, PM displayed good printing properties, water holding capacity, tensile strength, and elongation at break were increased. Tensile strength and elongation at break reached a maximum at 10 % IDF, and clearly similar results were found for texture attribute indices such as hardness, gumminess, chewiness, and cohesiveness after cooking. All printing inks exhibited shear-thinning behavior and solid-like viscoelasticity, but the structural recovery properties of 3D-printed PM deteriorated when the IDF content was over 10 %. Intermolecular forces indicated that the addition of IDF enhanced the disulfide bonds so that 10 % IDF presented better printing properties. These results indicated the potential for developing PM with dietary fiber functionality through 3D printing technology.