Formation Of Fibrous Structure Research Articles

Alaska pollock surimi-based meat analogs by high-moisture extrusion: Effect of konjac glucomannan/curdlan/carrageenan/sodium alginate on fibrous structure formation

This study investigated the effects of the addition of konjac glucomannan (KGM), curdlan (CD), carrageenan (CA), and sodium alginate (SA) on fibrous structure formation in surimi-based meat analogs to livestock meat. Meat analogs were prepared using high-moisture extrusion with Alaskan pollock surimi and soy protein isolate at a ratio of 7:3 (w/w). The meat analogs samples were labeled as SSP. Macrostructure observation showed that the best fibrous structure was obtained in SSP containing 2% SA. Mesostructure and microstructure observations revealed that 2% CD, CA or SA promoted the formation of a less tight three-dimensional network structure, which contributed to the formation of fiber filaments. Increased β-sheet structure content, ordered degree, fractal dimension and thermal stability were observed in SSP with the three colloids. Moreover, fibrous texture was closely associated with the thermal stability and fractal dimension. This study has provided useful information for colloid application in surimi-based meat analogs

Mechanism of l-cysteine-induced fibrous structural changes of soybean protein at different high-moisture extrusion zones

In this study, the fibrous structure formation mechanism of soybean protein during high moisture extrusion processing was investigated using a dead-stop operation, and based on the interaction between soybean protein concentrate (SPC) and L-cysteine (CYS). The thermal properties, SDS-PAGE and particle size distribution of the samples from different extrusion zones were investigated. It was revealed that the addition of a moderate amount of CYS (0.1 %) promoted the fibrous structure formation in the SPC extrudates and optimised the textural properties of the SPC extrudates. In the extruder barrel, addition of CYS (0.1 %) promoted protein depolymerisation and unfolding in the mixing and cooking zones, and facilitated protein aggregation in the die and cooling zones. Protein solubility and raman spectroscopy revealed that disulfide bonds were principally responsible for fibrous structure formation; favoured when the intermolecular disulfide bonds (t-g-t mode) was increased. Finally, the transformation of protein conformation was revealed by secondary structure and surface hydrophobicity, which confirmed that the effect of CYS on protein conformation mainly occurred in the cooling zone. This study provides a theoretical basis for the application of CYS to regulate the fibrous structure of meat analogues.

Effect of protease hydrolysis pretreatment on extruder response and the structural characteristics of high-moisture plant-protein extrudates

This study aimed to investigate the effect of protease hydrolysis pretreatment (PHP) on extruder response and the structural characteristics of high-moisture plant-protein extrudates. The results showed that specific mechanical energy of the extruder decreased from 147.06 kJ/kg to 116.14 kJ/kg, which reduced the energy consumption of the extruder and was beneficial for the application of hydrated wheat gluten with strong viscoelasticity during the extrusion process. Texturization degree that characterized the fibrous structure formation of high-moisture plant-protein extrudates reduced from 1.70 to 1.05. The hardness and chewiness decreased, while the springiness of the extrudates increased. Moderate PHP weakened the cross-linking strength and viscoelasticity of the extrudates, which can improve the problem of the excessively dense texture of high-moisture plant-protein extrudates. Meanwhile, PHP improved protein extractability and increased immobilized water and free water content in the extrudates.

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.

The Interactions of Soy Protein and Wheat Gluten for the Development of Meat-like Fibrous Structure.

Consumers who are environmentally and health conscious are increasingly looking for plant-based alternatives to replace animal-based products in their daily diets. Among these alternatives, there is a growing demand for meat analogues that closely resemble the taste and texture of meat. As a result, significant efforts have been dedicated to developing meat analogues with a desirable meat-like structure. Currently, soy protein and wheat gluten are the main ingredients used for producing these meat analogues due to their availability and unique functionalities. This study observed that high moisture extrusion at moisture levels of 50-80% has become a common approach for creating fibrous structures, with soy protein and wheat gluten being considered incompatible proteins. After the structuring process, they form two-phase filled gels, with wheat gluten acting as the continuous phase and soy protein serving as a filler material. Moreover, the formation of soy protein and wheat gluten networks relies on a combination of covalent and non-covalent interaction bonds, including hydrogen bonds that stabilize the protein networks, hydrophobic interactions governing protein chain associations during thermo-mechanical processes, and disulfide bonds that potentially contribute to fibrous structure formation. This review provides case studies and examples that demonstrate how specific processing conditions can improve the overall structure, aiming to serve as a valuable reference for further research and the advancement of fibrous structures.

Fate of pulse globulin proteins molecular Structure and composition on high moisture extrusion

Mungbean and lentil proteins are gaining attention for the production of high moisture extrusion (HME)-based meat- and dairy-analogues. However, understanding the mechanism of fibrous structure formation and molecular and higher-order changes in HME remains limited. Globulin protein isolates from mungbean (MBPI), green lentil (GLPI) and yellow pea (YPPI) along with commercial soy (CSPI) and yellow pea (CPPI) protein were investigated for their pasting properties using high-pressure rapid visco analyser (RVA), and the formation of anisotropic structures and molecular changes at constant HME conditions. Vicilin-rich MBPI showed higher viscosity on RVA, consumed higher specific mechanical energy (SME) during extrusion, and developed extrudates with higher textural strength and cutting force than proteins with both legumin and vicilin-like globulins, i.e. GLPI and YPPI. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and size-exclusion chromatography (SEC) of extrudates' soluble proteins showed dissociation of vicilin-like globulins into their smaller subunits. In contrast, legumin-like globulins were reaggregated into higher molecular weight soluble macromolecules. Further, SDS-PAGE of extrudates’ total protein revealed the involvement of legumin-like globulin in the macrostructure network of the extrudates. During HME, native unfolded structures were destroyed with conversion, predominately driving changes in the tertiary structure (thermal denaturation) and secondary structure with loss of helical structure to formation of random coil and beta-sheet structures. Protein extractability in different solvents was greatly reduced, with covalent and non-covalent interactions being majorly involved in the stabilisation of extrudates structure. Protein composition, and in particular vicilin-legumin ratio and protein conformation, determined the structural development and molecular changes in HME.

Electrospinning is a potential way for preparing edible plant protein-based nanofibers with porous surface using safflower seed meal

Food microstructure design has become an important research area in artificial food manufacturing. The fibrous structure is one of the most critical elements since it is the fundamental building blocks constructing the structure of several important food matrices. However, at present, edible fibers at nanoscale are seldomly successfully manufactured due to technical difficulties when only food-grade materials are allowed to be used. In the current study, edible nanofiber consisting of a single component of safflower seed meal protein (SMP) was prepared based on a three-step protocol consisting of electrostatic spinning, protein-cinnamaldehyde cross-linking, and subsequent immersion in the citric acid buffer to remove none-protein components. Addition of pullulan (PUL) to SMP during electrospinning facilitated fibrous structure formation. Results of SEM demonstrated that SMP: PUL = 5:5 with combined ratio 20% (w/v) in water is the upper limit to obtain well-structured composite nanofiber with no addition of Tween 80. In the second step, protein-cinnamaldehyde cross-linking was implemented to stabilize the structure of SMP. In the last step, citric acid buffer with pH4.6 was used to remove pullulan residues and thereafter nanofibers with porous surfaces composed of only SMP were successfully obtained. Our results showed that SMP single-component nanofibers had high thermal stability and good water-holding capacity, and thus suggesting that electrospinning can be a potentially innovative strategy to manufacture food fibrous microstructures especially at nanoscale.

Changes in physicochemical and structural properties of pea protein during the high moisture extrusion process: Effects of carboxymethylcellulose sodium and different extrusion zones

This study investigated effects of carboxymethylcellulose sodium (CMC) on the conformational evolution of pea protein during the high moisture extrusion process. The morphological observation showed that the addition of CMC facilitated the formation of fibrous structure of pea protein. In comparison with the pea protein in the melting zone and extrudate, the combination of CMC increased the denaturation enthalpy of pea protein by 2.09 % and 2.34 %. Compared with the material in the mixing zone, the degree of grafting between CMC and pea protein in the die was enhanced by 98.95 %. In general, the supplementation of CMC depressed the exposure of hydrophobic groups in the pea protein. In the extrusion barrel, the CMC increased the unfolding of protein molecular chains while it promoted the refolding of protein chains in the die. For the extrudate, the addition of CMC decreased the contents of α-helix and β-sheet of pea protein by 9.67 % and 6.93 % while the contents of β-turn and random coil were increased, leading to changes in the molecular weight distribution of protein molecules. In conclusion, these results provided new strategies toward producing the high-quality pea protein-based meat analogues by adding CMC.

Yeast protein-based meat analogues: Konjac glucomannan induces the fibrous structure formation by modifying protein structure

Carbohydrate polymers can induce the fibrous structure formation of meat analogues during high-moisture extrusion (HME). In this study, meat analogues were prepared using HME (60% moisture) from yeast protein (YP) and konjac glucomannan (KGM) blends. The impact of KGM (0, 1, 2, 4%, wet basis) addition on the textural, rheological, thermal, and structural properties of high-moisture meat analogues (HMMA) was investigated. The results indicated that KGM strengthened the hardness and chewiness and adjusted the formation and orientation of fibrous structures in HMMA. When the content of KGM reached 1%, the texture of HMMA was optimal. The rheological and thermal results showed that an appropriate KGM content (<4%) enhanced the structure of HMMA, which is consistent with the textural results. In addition, the structural results (ultraviolet–visible spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy, surface hydrophobicity, disulfide bond content, and X-ray diffraction) demonstrated that KGM increased the protein aggregation, β-sheet structure, S–S bond content, and ordered degree of HMMA, which were closely related to its texture and fibrous structure. The formation mechanism of KGM-induced fibrous structures in HMMA was preliminary clarified by the protein structure results. Moreover, the study suggested that YP in combination with KGM can be used to produce HMMA with a rich fibrous structure.

Study on high moisture extruded pea protein isolate based on acid-induced process: Physicochemical properties, conformational changes and fibrous structure mechanism

The present study aims to gain a better understanding of the physicochemical properties and quality attribute changes, and fibrous structure formation mechanisms of pea protein analogs with different glucan-δ-lactone (GDL) additions under high moisture extrusion. The results showed that the pH value of the extrudates gradually approached the isoelectric point and the zeta potential increased with the increase in GDL, which reduced the water holding capacity, nitrogen solubility index and browning index values, while increasing the hardness, chewiness and fibrous degree of the extrudates. The comparison revealed the maximum zeta potential value and total SH, and minimum free SH of the raw material, suggesting the unfolding and cross-linking of proteins under the triple action of the extruder. The relative content of β-sheet as the predominant component of protein extrudate decreased, while α-helix increased, and λmax was bathochromiclly shifted through FTIR and fluorescence spectroscopy. However, negative trends were observed when the GDL concentration reached 1%, due to the excessive concentration of the GDL accelerating the aggregation and sedimentation of proteins, and intensified the phase separation degree in the cooling die during the extrusion process, thus promoting the change in the velocity gradient. In addition, the thermal stability of the extrudate first increased and then decreased as the GDL concentration increased, and showed a three-step thermal degradation stage. The pores and highly irregular fibrous filaments transformed into a highly compact and coarse matrix with an excessive GDL concentration, as observed by SEM. These findings validate the potential of GDL to improve the textural attributes and structure formation of meat analogs, and provide a reference for the development of acid-induced proteins under high moisture extrusion.

High-moisture extrusion of yeast-pea protein: Effects of different formulations on the fibrous structure formation

The demand of meat analogues (MAs) is consistently increasing. The protein materials for MAs are primarily soy, pea, and wheat protein which can not completely meet the growing demand. Hence, this study is focused on the preparation of MAs with up to 50 % yeast protein (YP) instead of pea protein isolate (PPI). In the present study, 0 %, 10 %, 30 %, and 50 % YP powder in dry matter basis were combined with PPI; then the mixtures were used to prepare MAs with fibrous structures using high-moisture extrusion (55 % moisture). The involvement of YP significantly enhanced the hardness of MAs (P < 0.05). The optical and microstructural images illustrated that when YP ratio reached 30 %, obvious fibrous structures still were observed in MAs. Furthermore, MAs containing YP became whiter, which is conducive to reprocessing. With an increase in YP, the bound water content, sheet structures, and exposure of tryptophan residues in MAs increased, whereas the free water content, β-turn, and random coil structures decreased. Analysis of thermal and rheological behaviors indicated that YP lowered the denaturation temperature of MAs and the viscosity of protein dispersions, which was related to the formation of protein aggregates. Overall, YP can be used to prepare MAs and regulate the fibrous structure in MAs by acting on protein conformations.

A new strong and ductile multicomponent rare-earth free Mg–Bi-based alloy achieved by extrusion and subsequent short-term annealing

A new multicomponent rare-earth free low-alloyed Mg-1.0Bi-1.0Mn-1.0Al-0.5Ca-0.3Zn (wt.%) alloy is prepared by low-temperature and low-speed extrusion. The as-extruded sample has an ultra-high yield strength (∼425 MPa) but low elongation-to-failure (∼2.1%) mainly due to a bimodal grain structure containing ultra-fine recrystallized (DRXed) grains and large-sized unDRXed regions with a strong basal fiber texture feature, accompanied by a certain amount of micro-scale second phases (Al8Mn5 and Mg2Bi2Ca) and the uniformly distributed nano-scale α-Mn particles. More importantly, the excellent strength-ductility synergy is realized in the annealed samples after appropriate short-term annealing, and the yield strength and elongation-to-failure can reach ∼378 MPa and ∼16.8%, respectively. The effective inhibition of grain growth by grain boundary co-segregation of solutes and pinning effect of α-Mn nanoparticles is crucial for the annealed samples to maintain the relatively high strength. The formation of a new heterogeneous fibrous structure containing fine/coarse DRXed grains and thin fibrous unDRXed regions, along with weak basal fiber texture and low-density residual dislocations, is a key factor for the annealed sample to significantly enhance the ductility. Hence, such a new high strong and ductile low-alloyed Mg–Bi-based alloy will be helpful for enriching high performance low-cost wrought Mg alloy series to achieve extensive applications in industries.

Mechanism of high-moisture extruded protein fibrous structure formation based on the interactions among pea protein, amylopectin, and stearic acid

During high-moisture extrusion (HME) processing for plant protein texturization, the interactions among proteins, starch and lipids should determine the formation of fibrous structures, which has not been confirmed systematically. In this study, the mechanism of protein fibrous structure formation during HME processing (58% moisture) was investigated based on the intermolecular interactions among the pea protein, amylopectin and stearic acid. Results suggested that the amylopectin and stearic acid synergistically contributed to improve the fibrous structures such as the hardness and fibrous degree in pea protein extrudate. In the extruder barrel, the complexation among the protein with amylopectin and stearic acid gave rise to the formation of aggregates with higher thermal stability and delayed the formation of protein gel network. In the die, the amylopectin and stearic acid weakened the hydrogen bonds between proteins and hindered the aggregation of legumin and vicilin subunits. In the cooling zone and extrudate, the amylopectin and stearic acid promoted the formation of fibrous structures through an “anchor orientation and flexible cross-linking” mechanism. Namely, the stearic acid as anchors hindered the refolding of protein molecular chains, while the amylopectin promoted the rearrangement, cross-linking and aggregation of protein molecules. The amylopectin and stearic acid synergistically weakened the interaction forces between proteins and led to the formation of more flexible structures in aggregates, which was favorable for the orientation and formation of anisotropic fibrous structures in extrudates. This study provided a theoretical basis for the development and improvement of the plant-based meat substitutes.

An investigation of the wettability and chemical stability of superhydrophobic coatings on titanium

This study employs a two-step process to fabricate a superhydrophobic surface on the titanium substrate with outstanding corrosion resistance and chemical stability. Initially, a shot-peening treatment was carried out on the titanium surface, followed by chemical etching. Once the etching process was complete, the surface was modified with Methyltrichlorosilane (MTCS) to lower its surface energy. The impact of shot peening on wettability, corrosion resistance, and long-term chemical stability of the produced superhydrophobic surfaces was then investigated. Scanning electron microscopy images demonstrated the formation of fibrous network structure in the nanoscale, and Fourier transform infrared spectroscopy analysis confirmed the existence of chemical bonds between the functional groups of MTCS and the titanium surface. Furthermore, the corrosion resistance of the superhydrophobic surface was evaluated using immersion, potentiodynamic polarization, and an electrochemical impedance spectroscopy test in a 3.5 wt% NaCl solution. The long-term stability of the fabricated coating was tested by immersing samples in a 3.5 wt% NaCl solution for various immersion times. Based on the obtained results, the pre-shot peened samples exhibited a maximum water contact angle of 159° after MTCS modification. Furthermore, they also demonstrated excellent corrosion resistance and stability.

The Consistency Factor and the Viscosity Exponent of Soybean-Protein-Isolate/Wheat-Gluten/Corn-Starch Blends by Using a Capillary Rheometry.

Blends with different proportions of protein or starch show different rheological behaviors, which may be related to the fibrous structure formation of extruded textured plant proteins. The consistency factor K and the viscosity exponent n of soybean–protein–isolate (SPI)/wheat–gluten (WG)/corn–starch (CS) blends were investigated through capillary rheometry. All blends exhibited shear-thinning behavior at 80 °C and 50% moisture. The CS content in SPI/CS blends or WG content in SPI/WG blends showed a positive relation to the viscosity exponent n and a negative relation to the consistency factor K. However, there was no correlation between the CS content in WG/CS blends and n or K. The coefficient of determination of the linear relationship between K and mass fraction in SPI/CS, SPI/WG/CS, SPI/WG and WG/CS decreased from 0.872 to 0.073. SPI was more likely to form a non-interactive structure, while wheat-gluten was more likely to form a highly interactive structure. It turned out that the materials with globular morphology, such as soybean-protein-isolate and corn-starch, are likely to form a non-interactive structure.

Effect of pH and temperature on fibrous structure formation of plant proteins during high-moisture extrusion processing

This study investigated the effect of pH on fibrous structure formation (protein alignment) during high-moisture extrusion processing of gluten, rice protein, as well as pea protein concentrate, and isolate. The pH of the raw material was shifted to 5 and 7 in water suspension with an acid or base and freeze-dried, after which, conductivity, solubility, water-holding capacity, particle size, and pH were measured. The pH-shifted raw materials were extruded at various temperatures (95–160 °C) and the extrudates were analysed for protein alignment (macro and microstructure), tensile strength, free thiol groups, and cooking properties. In general, all raw materials generated fibrous structure at lower temperatures (115–140 °C) at pH 7 than at pH 5 (135–160 °C). Higher pH and temperature values led to an increased tensile strength and pronounced protein alignment. No such unambiguous link could be observed between the raw material properties and enhanced structure formation. This study showed that the structure formation of the extrudate can be positively influenced by increasing the pH of the raw material, which facilitates the plant protein structuring into appealing meat analogue products.

Nanocrystalline cellulose incorporated biopolymer tailored polyethersulfone mixed matrix membranes for efficient treatment of produced water

Membrane technology is a sustainable method to remove pollutants from petroleum wastewater. However, the presence of hydrophobic oil molecules and inorganic constituents can cause membrane fouling. Biomass derived biopolymers are promising renewable materials for membrane modification. In this study, fouling resistant biopolymer N-phthaloylchitosan (CS)- based polythersulfone (PES) mixed matrix membranes (MMMs) incorporated with nanocrystalline cellulose (NCC) was fabricated via phase inversion method and applied for produced water (PW) treatment. The morphological and Fourier-transform infrared spectroscopy (FTIR) analyses of the as-prepared NCC evidenced the formation of fibrous sheet-like structure and the presence of hydrophilic group. The membrane morphology and AFM analysis showed that the NCC altered the surface and cross-sectional morphology of the CS-PES MMMs. The tensile strength of NCC-CS-PES MMMs was also enhanced. 0.5 wt% NCC-CS-PES MMMs displayed a water permeability of 1.11 × 10−7 m/s.kPa with the lowest contact angle value of 61°. It affirmed that its hydrophilicity increased through the synergetic interaction between CS biopolymer and NCC. The effect of process variables such as transmembrane pressure (TMP) and synthetic produced water (PW) concentration were evaluated for both neat PES and NCC-CS-PES MMMs membranes. 0.5 wt% NCC-CS-PES MMMs exhibited the highest PW rejection of 98% when treating 50 mgL−1 of synthetic PW at a transmembrane pressure (TMP) of 200 kPa. The effect of nano silica and sodium chloride on the long-term PW filtration of NCC-CS-PES MMMs was also investigated.

Enzymatic modification of oat protein concentrate with trans- and protein-glutaminase for increased fibrous structure formation during high-moisture extrusion processing

Oat protein concentrate (OPC) was treated with transglutaminase (TG) and a combination of transglutaminase and protein-glutaminase (TG + PG), with or without preheating (95 °C, 15 min). The characteristics of the modified OPC were examined and further studied in high-moisture extrusion processing (HMEP). SDS-PAGE analysis showed that both enzyme preparations induced cross-linking between the OPC proteins and that the preheating step enhanced it. TG + PG treatments increased protein solubility and decreased the average particle size of OPC. TG treatment also decreased the particle size but had an insignificant effect on protein solubility. TG + PG 5 U treatment with preheating showed the highest RVA viscosity of 1076 mPa s. When OPC samples were studied during extrusion processing, enzyme treatments were found to affect the extrudate properties. The same OPC sample that showed the highest viscosity value, i.e. preheated TG + PG 5 U, showed also the most optimal fibrous structure formation and the strongest structure according to tensile strength results.

Egg white protein addition induces protein aggregation and fibrous structure formation of textured wheat gluten

The effect of egg white protein addition on the fibrous structure and protein aggregation of textured wheat gluten (TWG) extrudates was investigated. The hardness, springiness, chewiness, and degree of texturization of TWG significantly increased with the addition of egg white protein. Analysis of morphological characteristics showed a positive effect of egg white protein on the formation of the fibrous structure of TWG. The results of size-exclusion high performance liquid chromatography (SE-HPLC) indicated that the egg white protein improved the degree of wheat gluten aggregation, and the analysis of the protein intermolecular forces proved that disulfide bonds were the main contributor to the cross-linking of protein. In addition, an increase in the β-sheets also indicated an increase in protein aggregation induced by egg white protein. The addition of egg white protein promoted protein interactions and improved the fibrous structure of TWG.

The impact of phosphates on the fibrous structure formation of textured wheat gluten

Plant protein-based meat analogs have attracted attention as alternatives to meat products. To improve the fibrous structure of textured wheat gluten (TWG), different phosphates (sodium tripolyphosphate, sodium pyrophosphate, and sodium hexametaphosphate) were added to wheat gluten at different concentrations (0%, 0.25%, 0.5%, 1%, and 2%) during extrusion cooking. Analysis of the morphological characteristics showed the positive effect of sodium tripolyphosphate on the formation of the fibrous structure of TWG. The textural properties and degree of fibrous structure of TWG significantly improved with sodium tripolyphosphate treatment. Higher specific mechanical energy and lower bulk density were observed in the TWG treated with sodium pyrophosphate than in the control. The sodium dodecyl sulfate (SDS)-extractable protein results showed that sodium tripolyphosphate promoted the extent of gluten polymerization, but the other two phosphates had negative effects. The increased thermal stability of the sodium tripolyphosphate treatment group indicated stronger bonds conformation. The β-sheets content increased with sodium tripolyphosphate treatment. X-ray photoelectron spectroscopy results showed that the phosphate group was successfully introduced into the TWG treated with sodium tripolyphosphate via a phosphorylation reaction. The decrease in elastic modulus and viscous modulus observed with sodium tripolyphosphate treatment was related to changes in surface charges and the water layer of protein, which were affected by PO43−. Thus, sodium tripolyphosphate is a promising candidate that can be used for the improvement of the fibrous structure of TWG.