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1.
Food Res Int ; 188: 114503, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823881

ABSTRACT

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.


Subject(s)
Cooking , Gliadin , Glutens , Hot Temperature , Triticum , Glutens/chemistry , Triticum/chemistry , Cooking/methods , Gliadin/chemistry , Polymerization , Water/chemistry
2.
Molecules ; 29(9)2024 May 02.
Article in English | MEDLINE | ID: mdl-38731596

ABSTRACT

This work aimed to develop gluten-free snacks such as crispbread based on beetroot pomace (Beta vulgaris L.) and golden linseed (Lini semen). Beetroot is attracting more and more consumer attention because of its nutritional and health properties. The use of beet pomace contributes to waste management. Linseed, known as a superfood with many health-promoting properties, was used to produce crispbreads as an alternative to cereals, which are allergens. Beetroot pomace and whole or ground linseed were used in different proportions to produce crispbread snacks. Chemical and physical analyses were performed including water activity, dry matter, betalains, and polyphenols content, as well as Fourier transform infrared spectroscopy (FTIR). A sensory evaluation and microstructure observations were also performed. The obtained snacks were characterized by low water activity (0.290-0.395) and a high dry matter content (93.43-97.53%), which ensures their microbiological stability and enables longer storage. Beetroot pomace provided betalains-red (14.59-51.44 mg betanin/100 g d.m.) and yellow dyes (50.02-171.12 mg betanin/100 g d.m.)-while using linseed enriched the product with polyphenols (730-948 mg chlorogenic acid/100 g d.m.). FTIR analysis showed the presence of functional groups such as the following: -OH, -C-O, -COOH, and -NH. The most desired overall consumer acceptability was achieved for snacks containing 50% beetroot pomace and 50% linseed seeds. The obtained results confirmed that beetroot pomace combined with linseed can be used in the production of vegetable crispbread snacks.


Subject(s)
Beta vulgaris , Flax , Snacks , Beta vulgaris/chemistry , Flax/chemistry , Vegetables/chemistry , Betalains/chemistry , Betalains/analysis , Polyphenols/analysis , Polyphenols/chemistry , Spectroscopy, Fourier Transform Infrared , Diet, Gluten-Free , Phytochemicals/chemistry , Glutens/analysis , Glutens/chemistry
3.
J Agric Food Chem ; 72(19): 11080-11093, 2024 May 15.
Article in English | MEDLINE | ID: mdl-38690996

ABSTRACT

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.


Subject(s)
Amyloid , Cooking , Glutens , Triticum , Glutens/chemistry , Triticum/chemistry , Amyloid/chemistry , Gliadin/chemistry , Hot Temperature , Protein Aggregates , Molecular Weight , X-Ray Diffraction
4.
Food Chem ; 451: 139512, 2024 Sep 01.
Article in English | MEDLINE | ID: mdl-38718641

ABSTRACT

In view of the merits of all-purpose wheat flour (APWF) to soft wheat flour (SWF) in cost and protein supply, the feasibility of heat-moisture treatment (HMT, 19% moisture for 1 h at 60, 80 and 100 °C, respectively) to modify APWF as a substitute SWF in making short dough biscuits was explored. For underlying mechanisms, on the one hand, HMT reduced the hydration capacity of damaged starch particles by coating them with denatured proteins. On the other hand, HMT at 80 °C and 100 °C significantly denatured gluten proteins to form protein aggregates, highly weakening the gluten network in dough. These two aspects jointly conferred APWF dough with higher deformability and therefore significantly improved the qualities of biscuits. Moreover, the qualities of biscuits from APWF upon HMT-100 °C were largely comparable to that from SWF, even higher values were concluded in spread ratio, volume, specific volume and consumer acceptance.


Subject(s)
Bread , Flour , Food Handling , Hot Temperature , Triticum , Flour/analysis , Triticum/chemistry , Bread/analysis , Glutens/chemistry , Water/chemistry , Humans
5.
Food Chem ; 452: 139562, 2024 Sep 15.
Article in English | MEDLINE | ID: mdl-38749140

ABSTRACT

The growing global interest in physical and environmental health has led to the development of plant-based products. Although soy protein and wheat gluten are commonly utilized, concerns regarding gluten-related health issues have driven exploration into alternative proteins. Zein has emerged as a promising option. This research investigated the impact of extraction methods on zein characteristics and the structures of SPI-zein composite gels. Different extraction methods yielded zein with protein contents ranging from 48.12 % to 64.34 %. Ethanol-extracted Z1 and Z3, obtained at different pH conditions, exhibited zeta potential of -3.25 and 5.43 mV, respectively. They displayed similar characteristics to commercial zein and interacted comparably in composite gels. Conversely, alkaline-extracted Z2 had a zeta potential of -2.37 mV and formed distinct gels when combined with SPI. These results indicated that extraction methods influence zein behaviour in composite gels, offering possibilities for tailored formulations and expanding zein's applications, particularly in gluten-free plant-based products.


Subject(s)
Gels , Zein , Zein/chemistry , Gels/chemistry , Glutens/chemistry , Glutens/isolation & purification , Triticum/chemistry , Soybean Proteins/chemistry , Soybean Proteins/isolation & purification
6.
Food Chem ; 453: 139676, 2024 Sep 30.
Article in English | MEDLINE | ID: mdl-38776795

ABSTRACT

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.


Subject(s)
Anthocyanins , Blueberry Plants , Food Packaging , Glutens , Triticum , Blueberry Plants/chemistry , Anthocyanins/chemistry , Glutens/chemistry , Animals , Triticum/chemistry , Food Packaging/instrumentation , Antioxidants/chemistry
7.
Food Chem ; 453: 139709, 2024 Sep 30.
Article in English | MEDLINE | ID: mdl-38781908

ABSTRACT

As an emerging physical technology, magnetic fields have been used to improve the quality of frozen and refrigerated foods. This study compared the effect of applying a static magnetic field (2 mT) at different stages of freezing and storage on the quality of frozen dough. Results suggested that the magnetic field significantly impacted frozen dough quality. It not only prevented the formation of ice crystals during the pre-freezing stage but also inhibited ice crystal growth during the following frozen storage. This effect helped to maintain the integrity of gluten proteins and their adhesion to starch granules by preventing the breakage of disulfide bonds and the depolymerization of gluten macromolecules. It was also observed that yeast inactivation and glutathione release were reduced, resulting in improved air retention and air production capacity of the dough. This, in turn, led to a more appealing volume and texture quality of the finished bread.


Subject(s)
Bread , Flour , Freezing , Magnetic Fields , Triticum , Triticum/chemistry , Bread/analysis , Flour/analysis , Glutens/chemistry , Glutens/analysis , Cooking
8.
Food Chem ; 453: 139598, 2024 Sep 30.
Article in English | MEDLINE | ID: mdl-38754351

ABSTRACT

In this study, dynamic behaviors of proteins and water during fresh noodles processing associated with the quality of fresh noodles were systematically investigated by using wheat near-isogenic lines carrying high-molecular-weight glutenin subunits (HMW-GS) 2 + 12, 3 + 12 or 5 + 10 at the Glu-D1 locus. The results showed that subunits 5 + 10 tend to form a complex gluten network and had a poorly hydrated ability, that prevent the intrusion of external water during cooking; subunits 3 + 12 formed a moderate strength gluten network that generated a medium ability to resist the hydrated and mechanical treatment, which explained the highest water absorption and less cooking loss of cooked noodles; while subunits 2 + 12 formed fragile protein aggregates that had a poor ability to resist mechanical. The findings demonstrated that subunits 3 + 12 provided a suitable gluten network which was crucial for intrusion and hydration of external water thus formed a uniform gluten network and excellent fresh noodle quality.


Subject(s)
Cooking , Glutens , Molecular Weight , Triticum , Water , Glutens/chemistry , Triticum/chemistry , Water/chemistry , Flour/analysis , Plant Proteins/chemistry , Food Handling
9.
Compr Rev Food Sci Food Saf ; 23(3): e13353, 2024 05.
Article in English | MEDLINE | ID: mdl-38660747

ABSTRACT

Deterioration of bread quality, characterized by the staling of bread crumb, the softening of bread crust and the loss of aroma, has caused a huge food waste and economic loss, which is a bottleneck restriction to the development of the breadmaking industry. Various bread improvers have been widely used to alleviate the issue. However, it is noteworthy that the sourdough technology has emerged as a pivotal factor in this regard. In sourdough, the metabolic breakdown of carbohydrates, proteins, and lipids leads to the production of exopolysaccharides, organic acids, aroma compounds, or prebiotics, which contributes to the preeminent ability of sourdough to enhance bread attributes. Moreover, sourdough exhibits a "green-label" feature, which satisfies the consumers' increasing demand for additive-free food products. In the past two decades, there has been a significant focus on sourdough with in situ produced dextran due to its exceptional performance. In this review, the behaviors of bread crucial compositions (i.e., starch and gluten) during dough mixing, proofing, baking and bread storing, as well as alterations induced by the acidic environment and the presence of dextran are systemically summarized. From the viewpoint of starch and gluten, results obtained confirm the synergistic amelioration on bread quality by the coadministration of acidity and dextran, and also highlight the central role of acidification. This review contributes to establishing a theoretical foundation for more effectively enhancing the quality of wheat breads through the application of in situ produced dextran.


Subject(s)
Bread , Dextrans , Glutens , Starch , Triticum , Bread/analysis , Bread/standards , Starch/chemistry , Glutens/chemistry , Dextrans/chemistry , Triticum/chemistry , Fermentation , Food Handling/methods , Food Quality
10.
J Proteome Res ; 23(5): 1649-1665, 2024 May 03.
Article in English | MEDLINE | ID: mdl-38574199

ABSTRACT

Plant-based adhesives, such as those made from wheat, have been prominently used for books and paper-based objects and are also used as conservation adhesives. Starch paste originates from starch granules, whereas flour paste encompasses the entire wheat endosperm proteome, offering strong adhesive properties due to gluten proteins. From a conservation perspective, understanding the precise nature of the adhesive is vital as the longevity, resilience, and reaction to environmental changes can differ substantially between starch- and flour-based pastes. We devised a proteomics method to discern the protein content of these pastes. Protocols involved extracting soluble proteins using 0.5 M NaCl and 30 mM Tris-HCl solutions and then targeting insoluble proteins, such as gliadins and glutenins, with a buffer containing 7 M urea, 2 M thiourea, 4% CHAPS, 40 mM Tris, and 75 mM DTT. Flour paste's proteome is diverse (1942 proteins across 759 groups), contrasting with starch paste's predominant starch-associated protein makeup (218 proteins in 58 groups). Transformation into pastes reduces proteomes' complexity. Testing on historical bookbindings confirmed the use of flour-based glue, which is rich in gluten and serpins. High levels of deamidation were detected, particularly for glutamine residues, which can impact the solubility and stability of the glue over time. The mass spectrometry proteomics data have been deposited to the ProteomeXchange, Consortium (http://proteomecentral.proteomexchange.org) via the MassIVE partner repository with the data set identifier MSV000093372 (ftp://MSV000093372@massive.ucsd.edu).


Subject(s)
Adhesives , Flour , Glutens , Proteome , Starch , Triticum , Triticum/chemistry , Flour/analysis , Starch/chemistry , Proteome/analysis , Proteome/chemistry , Adhesives/chemistry , Glutens/chemistry , Glutens/analysis , Proteomics/methods , Plant Proteins/analysis , Gliadin/chemistry , Gliadin/analysis
11.
Int J Biol Macromol ; 267(Pt 1): 131402, 2024 May.
Article in English | MEDLINE | ID: mdl-38582462

ABSTRACT

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.


Subject(s)
Glutens , Hot Temperature , Salicylic Acid , Tensile Strength , Salicylic Acid/chemistry , Glutens/chemistry , Solubility , Water/chemistry , Triticum/chemistry , Spectroscopy, Fourier Transform Infrared
12.
Food Chem ; 450: 139219, 2024 Aug 30.
Article in English | MEDLINE | ID: mdl-38640531

ABSTRACT

Foxtail millet and sourdough are used to make foxtail millet sourdough steamed bread to improve the flavor and taste. Compared with the conventional freeze-thaw treatment (CFT), the effect of magnetic field-assisted freeze-thaw treatment (MFT) on the storage quality of foxtail millet sourdough and steamed bread is explored. The results showed that compared with CFT, MFT shortened the phase transition time of dough; decreased the water loss rate, the water mobility, and the freezable water content; increased the fermentation volume; stabilized the rheological properties; and minimized the damage of freezing and thawing to the secondary structure and microstructure of the gluten. In addition, an analysis of the specific volume, texture, surface color, and texture structure showed that MFT was beneficial to slowing the deterioration of the steamed bread texture. Finally, MFT effectively inhibited the growth and recrystallization of ice crystals during freezing and thawing, improving the quality of millet dough and steamed bread.


Subject(s)
Bread , Freezing , Setaria Plant , Taste , Bread/analysis , Setaria Plant/chemistry , Setaria Plant/growth & development , Food Handling , Fermentation , Flour/analysis , Magnetic Fields , Glutens/chemistry , Glutens/analysis , Rheology
13.
Int J Biol Macromol ; 269(Pt 1): 131907, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38677676

ABSTRACT

This study incorporated citrus pectin in wheat bread, aiming to develop breads with both desirable texture and slow starch digestibility. Results showed that starch digestibility in wheat bread decreased over the addition of pectin, and the maximum starch digested amount decreased by 6.6 % after the addition of 12 % pectin (wheat flour weight basis). The addition of pectin transferred part of the rapidly digestible starch into slowly digestible starch, and reduced the binding rate constant between slowly digestible starch and digestive enzymes, resulting in overall reduced starch digestibility. Furthermore, the addition of 4 % pectin contributed to the development of wheat bread with softer texture and increased specific volume. Mechanistically, the lowered starch digestibility of wheat bread after the pectin addition was due to (1) residual outermost swollen layer of starch granules, (2) protein and pectin interactions, and (3) increased short-range ordering of starch. This study, therefore, suggests that the addition of an appropriate amount of citrus pectin has the potential to develop bread with both a low glycemic index and desirable texture.


Subject(s)
Bread , Glutens , Pectins , Starch , Triticum , Pectins/metabolism , Pectins/chemistry , Bread/analysis , Starch/metabolism , Starch/chemistry , Glutens/chemistry , Glutens/metabolism , Triticum/chemistry , Triticum/metabolism , Digestion , Flour/analysis
14.
Food Funct ; 15(9): 5132-5146, 2024 May 07.
Article in English | MEDLINE | ID: mdl-38682288

ABSTRACT

Growing demand for sustainable, plant-based protein sources has stimulated interest in new ingredients for food enrichment. This study investigates the nutritional and digestive implications of enriching wheat dough with RuBisCO, in comparison to pea protein-enriched and gluten-enriched doughs. The protein quality and digestibility of these enriched doughs were analysed through dough characterization, in vitro digestion experiments and biochemical analysis of digesta. Our findings indicate that an enrichment at 10% of RuBisCO or pea proteins improves the chemical score and the in vitro PDCAAS (IV-PDCAAS) score of wheat dough as compared to the control dough. Digestibility assays suggest that RuBisCO introduction modifies the protein hydrolysis kinetics: the nitrogen release is lower during gastric digestion but larger during intestinal digestion than other samples. The analysis of the protein composition of the soluble and insoluble parts of digesta, using size-exclusion chromatography, reveals that the protein network in RuBisCO-enriched dough is more resistant to gastric hydrolysis than the ones of other doughs. Indeed, non-covalently bound peptides and disulfide-bound protein aggregates partly composed of RuBisCO subunits remain insoluble at the end of the gastric phase. The digestion of these protein structures is then mostly performed during the intestinal phase. These results are also discussed in relation to the digestive enzymatic cleavage sites, the presence of potential enzyme inhibitors, the protein aggregation state and the secondary structures of the protein network in each dough type.


Subject(s)
Digestion , Glutens , Ribulose-Bisphosphate Carboxylase , Triticum , Ribulose-Bisphosphate Carboxylase/metabolism , Ribulose-Bisphosphate Carboxylase/chemistry , Triticum/chemistry , Triticum/metabolism , Glutens/metabolism , Glutens/chemistry , Flour/analysis , Pea Proteins/chemistry , Pea Proteins/metabolism , Pisum sativum/chemistry , Hydrolysis , Humans , Plant Proteins/metabolism , Plant Proteins/chemistry
15.
Int J Biol Macromol ; 267(Pt 1): 131690, 2024 May.
Article in English | MEDLINE | ID: mdl-38688790

ABSTRACT

In the current study, how pectin retards the digestibility of wheat gluten was investigated using a static in vitro gastric-duodenal model. The degree of protein hydrolysis was estimated using the o-phthaldialdehyde method, while the in vitro digestograms were mathematically fitted using a single first-order kinetics model. Peptides' profile, free amino acids compositions, gluten-pectin interactions and their effects on enzymatic activities of proteolytic enzymes as well as on the gluten secondary structures under digestive conditions were studied using combined techniques. Results showed that pectin could retard gluten digestibility through 1). preferential absorption to insoluble gluten aggregates by electrostatic interactions; 2). increasing the helix and reducing the ß-sheet content of the solubilized gluten protein fractions in terms of their secondary molecular structures; 3). reducing pepsin activity by forming negatively charged pectin-gluten mixtures which then interacted with the positively charged pepsin molecules. The deeper insight into gluten-pectin interactions and their influences on gluten digestibility under gastrointestinal conditions provides important clues for developing effective forms of dietary fiber to improve the nutritional benefits of plant protein in individuals.


Subject(s)
Digestion , Glutens , Pectins , Pepsin A , Pectins/chemistry , Pectins/pharmacology , Glutens/chemistry , Digestion/drug effects , Hydrolysis , Pepsin A/chemistry , Pepsin A/metabolism , Duodenum/metabolism , Duodenum/drug effects , Triticum/chemistry , Proteolysis , Amino Acids/chemistry , Kinetics
16.
Food Chem ; 446: 138856, 2024 Jul 15.
Article in English | MEDLINE | ID: mdl-38430765

ABSTRACT

In this study, we examined the effects of various sodium alginate (ALG) concentrations (0.2%-0.8%) on the functional and physicochemical characteristics of succinylated walnut glutenin (GLU-SA). The results showed that acylation decreased the particle size and zeta potential of walnut glutenin (GLU) by 122- and 0.27-fold, respectively. In addition, the protein structure unfolded, providing conditions for glycosylation. After GLU-SA was combined with ALG, the surface hydrophobicity decreased and the net negative charge and disulfide bond content increased. The protein structure was analyzed by FTIR, Endogenous fluorescence spectroscopy, and SEM, and ALG prompted GLU-SA cross-linking to form a stable three-dimensional network structure. The results indicated that dual modification improved the functional properties of the complex, especially its potential protein gel and emulsifying properties. This research provide theoretical support and a technical reference for expanding the application of GLU in the processing of protein and oil products.


Subject(s)
Juglans , Juglans/chemistry , Glycosylation , Glutens/chemistry , Nuts/chemistry
17.
J Texture Stud ; 55(2): e12826, 2024 Apr.
Article in English | MEDLINE | ID: mdl-38528687

ABSTRACT

The texture properties after cooking for 12 min were selected to optimize the sheeting parameters, and the results were verified using the comprehensive quality of dried noodles. The distribution of water, characteristics of gluten protein, and interaction between gluten network and starch were analyzed to clarify the mechanism of the quality of dried noodles. Results showed that the optimal folding angle was 45°, under this condition, the largest anti-extension displacement perpendicular to the rolling direction and the smallest cooking loss were obtained. The hardness and smoothness of cooked noodles increased by about 14% to 17%. Further, the transverse relaxation time of strongly bound water significantly decreased, while the relative content and binding strength increased. The hydrogen bonds and α-helix contents increased by about 68.8% and 53.1%, respectively. Folding and sheeting enhanced the combination of starch granules and gluten network causing, decreased in the average length and porosity of the gluten network. It is depicted from the results that the method of optimizing the sheeting process based on the texture of dried noodles cooked for 12 min was feasible. And the 45° folding and sheeting could help to improve the quality of dried noodles.


Subject(s)
Flour , Glutens , Glutens/chemistry , Flour/analysis , Cooking , Starch/chemistry , Water/chemistry
18.
Food Chem ; 448: 139025, 2024 Aug 01.
Article in English | MEDLINE | ID: mdl-38522293

ABSTRACT

Monitoring of the accidental presence of gluten (Glu), resulting from cross-contamination, is imperative in different industries, in particular food industry. The objective of this study was the development of an analytical platform utilizing thin-layer chromatography (TLC) with colorimetric read-out for making binary (yes/no) decisions on surfaces and/or point of these industries. The composition of the extractive phase was optimized with commercial products used in cleaning processing lines. Subsequently, an exploration of TLC separation and detection was undertaken. CN-modified nanosilica plates and 30:70 acetonitrile:water were used to achieve a selective signal for Glu residues. The study of the detection performance showed that both spectroscopic measurement and image analysis were resulted in satisfactory results for quantitate analysis (RSD = 5 %, LOD = 0.12 mg). The practical application of the proposed methodology on surfaces of the food processing lines. This work demonstrated the operational feasibility in detecting gluten cross-contaminations within the food processing industry.


Subject(s)
Colorimetry , Food Contamination , Glutens , Food Contamination/analysis , Glutens/analysis , Glutens/chemistry , Colorimetry/methods , Chromatography, Thin Layer/methods , Food Industry
19.
Food Chem ; 448: 139103, 2024 Aug 01.
Article in English | MEDLINE | ID: mdl-38547708

ABSTRACT

The protein content (PC) and wet gluten content (WGC) are crucial indicators determining the quality of wheat, playing a pivotal role in evaluating processing and baking performance. Original reflectance (OR), wavelet feature (WF), and color index (CI) were extracted from hyperspectral and RGB sensors. Combining Pearson-competitive adaptive reweighted sampling (CARs)-variance inflation factor (VIF) with four machine learning (ML) algorithms were used to model accuracy of PC and WGC. As a result, three CIs, six ORs, and twelve WFs were selected for PC and WGC datasets. For single-modal data, the back-propagation neural network exhibited superior accuracy, with estimation accuracies (WF > OR > CI). For multi-modal data, the random forest regression paired with OR + WF + CI showed the highest validation accuracy. Utilizing the Gini impurity, WF outweighed OR and CI in the PC and WGC models. The amalgamation of MLs with multimodal data harnessed the synergies among various remote sensing sources, substantially augmenting model precision and stability.


Subject(s)
Algorithms , Glutens , Machine Learning , Plant Proteins , Triticum , Triticum/chemistry , Glutens/analysis , Glutens/chemistry , Plant Proteins/analysis , Plant Proteins/chemistry
20.
Food Chem ; 447: 138932, 2024 Jul 30.
Article in English | MEDLINE | ID: mdl-38484546

ABSTRACT

The thawing method is critical for the final quality of products based on the frozen dough. The effects of ultrasound thawing, proofer thawing, refrigerator thawing, water bath thawing, ambient thawing, and microwave thawing on the rheology, texture, water distribution, fermentation characteristics, and microstructure of frozen dough and the properties of steamed bread were investigated. The results indicated that the ultrasound thawing dough had better physicochemical properties than other doughs. It was found that ultrasound thawing restrained the water migration of dough, improved its rheological properties and fermentation capacity. The total gas volume value of the ultrasound thawing dough was reduced by 21.35% compared with that of unfrozen dough. The ultrasound thawing dough displayed a thoroughly uniform starch-gluten network, and an enhanced the specific volume and internal structure of the steamed bread. In conclusion, ultrasound thawing effectively mitigated the degradation of the frozen dough and enhanced the quality of steamed bread.


Subject(s)
Bread , Steam , Bread/analysis , Water/chemistry , Glutens/chemistry , Freezing , Flour/analysis
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