Protein Gel Research Articles

Viscosity, mixing regime and power consumption analysis during enzymatic hydrolysis of fish (Sardina pilchardus) processing by-products, through development of power number and Reynolds number correlations

The influence of processing conditions on fluid rheology and mixing regime is of considerable importance during enzymatic hydrolysis of fish processing by-products. Solids concentration ranging from 30 to 70 % (wet basis) and mixing speed from 100 to 400 rpm were investigated, with apparent viscosity, power consumption, power number (Np) and Reynolds number (Re) as response variables of interest. The fish processing by-products at different solids concentration showed power-law pseudoplastic behaviour. Apparent viscosity ranged from 4.35 to 8.51 mPa·s, and power consumption ranged from 53.0 to 492 W/m3. Np―Re curves showed the typical relationship where Np decreased from 20.4 to 1.99 when Re increased from 425 to 3 317. Poor mixing was observed at high solids concentration and low mixing speed, with cavern formation in the early stages of mixing. Liquefaction of solids led to the disappearance of caverns, resulting in good degree of mixing during the hydrolysis process. Contrary to expectations, our study indicated that liquefaction of solids and reduction in molecular weight of proteins had a significant effect on power consumption more than increase in soluble protein concentration, gel formation and/or emulsion. Liquefaction and molecular weight reduction caused a decrease in fluid viscosity while increase in protein concentration, gel formation and/or emulsion contributed to an increase in viscosity. The net result was a decrease in power consumption from 0 to 60 min of enzymatic hydrolysis. The practical implications of the results presented in this study are that one Np―Re curve can be used for any solids concentration between 30 and 50 %. Beyond 50 %, low degree of hydrolysis, protein recovery and significantly high power consumption are experienced.

Gel properties and in vitro digestion of sea bass (Lateolabrax japonicus) myofibrillar protein – Lipid composite gels: Focus on lipid type and content

The effects of lipid type and content on gel and digestion properties of myofibrillar proteins (MPs) were studied. The MPs sol was combined with three types of lipid (peanut oil, sunflower oil, and lard) with different contents (0.5–2%) to obtain composite gels. As for whiteness, no differ was observed in composite gels without or with lipid addition. The water holding capacity and hardness of composite gels with lipid addition increased. Moreover, fourier transform infrared spectra (FTIR) demonstrated composite gels with 1% emulsion addition exhibited the highest β-sheet content. The confocal laser scanning microscope (CLSM) revealed that networks of composite gels with 1% emulsion addition possessed more densely compared to control group. During the in vitro digestion, high performance liquid chromatography (HPLC) results showed the peptide (>10 kDa) contents of composite gels with lipid addition were lower than that of control group under the simulated gastric phase. Moreover, the 2–5 kDa polypeptide content of composite gels with lipid addition was higher than that in observed in control group under intestinal phase. The results illustrated the gel and in vitro digestion mechanism of composite gels with lipid addition, which can be valuable for the fabrication of functional surimi products.

Protein Stability in Pasteurized Cow and Goat Milk using Protein Gel Electrophoresis

Milk is a nutritious beverage that contains whey, casein, and milk fat globule membrane (MFGM) proteins. Pasteurization kills pathogenic microorganisms in milk, making it safe to drink. A high heat load during processing can affect the protein quality of milk. In this study, protein gel electrophoresis (Native and SDS-PAGE) was used to view the protein profiles of retail cow and goat milk samples pasteurized at different temperatures (145, 165, or 280 °F) compared to commercially spray dried milk (356–482 °F). SDS-PAGE provided better resolution of the milk proteins compared to Native-PAGE. There were clear species differences in the MFGM proteins. This could be used to spot adulteration of goat milk with cow milk, however none of the samples showed signs of adulteration. There were no overt patterns of protein degradation with increasing pasteurization temperature. However drying reduced band intensity, especially MFGM and whey proteins in the goat milk sample. Whereas most samples came from different herds where genetics and environmental conditions varied, two of the goat milk samples were from the same herd, one fresh and one spray dried. It was evident from these two samples that spray drying can alter proteins in goat milk. Even so, if fresh milk is unavailable or unaffordable, dry milk remains a valuable protein source.

Effect and Mechanism of Soluble Starch on Bovine Serum Albumin Cold-Set Gel Induced by Microbial Transglutaminase: A Significantly Improved Carrier for Active Substances.

Soluble starch (SS) could significantly accelerate the process of bovine serum albumin (BSA) cold-set gelation by glucono-δ-lactone (GDL) and microbial transglutaminase (MTGase) coupling inducers, and enhance the mechanical properties. Hardness, WHC, loss modulus (G″) and storage modulus (G') of the gel increased significantly, along with the addition of SS, and gelation time was also shortened from 41 min (SS free) to 9 min (containing 4.0% SS); the microstructure also became more and more dense. The results from FTIR, fluorescence quenching and circular dichroism (CD) suggested that SS could bind to BSA to form their composites, and the hydrogen bond was probably the dominant force. Moreover, the ability of SS to bind the original free water in BSA gel was relatively strong, thereby indirectly increasing the concentration of BSA and improving the texture properties of the gel. The acceleration of gelling could also be attributed to the fact that SS reduced the negative charge of BSA aggregates and further promoted the rapid formation of the gel. The embedding efficiency (EE) of quercetin in BSA-SS cold-set gel increased from 68.3% (SS free) to 87.45% (containing 4.0% SS), and a controlled-released effect was detected by simulated gastrointestinal digestion tests. The work could put forward new insights into protein gelation accelerated by polysaccharide, and provide a candidate for the structural design of new products in the food and pharmaceutical fields.

Protein oxidation/aggregation during ultrasound thawing at different powers impair the gel properties of common carp (Cyprinus carpio) myofibrillar protein

The influences of ultrasound thawing (UT) at different power (0, 100, 300, and 500 W) on the oxidation, aggregation, and gel properties of common carp (Cyprinus carpio) myofibrillar protein were evaluated in the present study. The free amino content, carbonyl content, dityrosine content, and TBARS value of UT-300 were significantly lower than those of other thawing groups (P < 0.05), suggesting that appropriate ultrasound power (300 W) thawing inhibited the oxidation of myofibrillar protein and fat. However, excessive power (500 W) UT enhanced the oxidation of fish protein. UT-300 had the smallest surface hydrophobicity, particle size, and turbidity values, indicating that UT-300 reduced protein aggregation caused by thawing. At the same time, UT-300 protein gel had a higher gel strength and water-holding capacity than other thawing treatments, which were characterized by fine and uniform gel networks. Water distribution analysis also proved that UT-300 inhibited the loss of bound water, free water, and immobilized water, as well as the increase in fluidity caused by thawing. In conclusion, proper power (300 W) UT was beneficial in inhibiting the degradation of gel properties caused by protein oxidation and aggregation during thawing.

Improving the gelation and digestive properties of myofibrillar protein in Litopenaeus vannamei by ultra-high pressure

The objective of this study was to investigate the effects of ultra-high pressure (UHP) on the physicochemical properties, gelling properties, and in vitro digestion characteristics of myofibrillar protein (MP) in Litopenaeus vannamei. The pressures were set at 0, 150, 300, 450, and 600 MPa, respectively. The α-helix structure gradually unfolded and transformed into β-sheet structure as the pressure increased from 0 to 600 MPa. Compared with the control group, the content of α-helix structure of the 600 MPa-treated MP samples decreased by 51.31%, and the content of β-sheet structure increased by a 1.34-fold. In addition, the UHP treatment enhanced the rheological properties of MP. The elastic modulus (G′) and viscous modulus (G″) of the 600 MPa-treated MP samples increased by 4.77-fold and 3.78-fold, respectively, compared with the control group (at frequencies up to 10 Hz). The gel properties of the MP also increased significantly after UHP treatment, e.g., the WHC of MP gel increased by 45.49% and the gel strength increased by a 5.99-fold when the pressure reached 600 Mpa, compared with the control group. The results of in vitro simulated digestion showed that UHP treatment led to the formation of more easily digestible MP gels. Compared with the control group, the 600 MPa-treated MP gel samples showed a 1.89-fold increase in digestibility and a 66.86% decrease in digestible particle size.

Effect of fining agents on the chemical composition and sensory properties of apple cider

This study focuses on analyzing the impact of various fining agents on apple cider and evaluating their effects on its physical–chemical and sensory properties. Despite its common cloudy state, some consumers prefer clear apple cider. Within this study, two variations of apple cider were analyzed: original cider and cider with added barrique extract. Eight different fining agents were applied to these samples, specifically bentonite, gelatin, polyvinylpolypyrrolidone, egg white protein, activated carbon, pea protein, isinglass, and silica gel. The results revealed that the use of fining agents significantly impacted the antioxidant content in apple cider. The most substantial reduction in antioxidants was observed in samples with added activated carbon, resulting in a 75% decrease to values of 0.11–0.26 mmol TE/L. This decrease in antioxidants correlated with a decline in total polyphenols. Sensory analysis demonstrated statistically significant differences among the various apple cider samples. Bentonite and egg white protein had minimal adverse effects on sensory properties, while activated carbon had the most pronounced negative impact on the aroma and taste of the cider. This study provides valuable insights into the use of fining agents in winemaking technology and their effects on the quality of apple cider, considering consumer preferences.

Entrapment of curcumin in hydrogels of whey peptides and its release during static in vitro gastrointestinal digestion

The suitability of a whey peptide hydrogel for entrapping curcumin compared with a whey protein isolate (WPI) gel was investigated. In addition, the release of curcumin entrapped in the peptide and protein gels was evaluated during static in vitro gastrointestinal digestion. The peptide hydrogel showed a 91% entrapment efficiency of curcumin compared with 99.9% for the WPI gel and at the end of intestinal digestion curcumin retention was close to 98% in the peptide hydrogel, whereas it was only 90% for the WPI gel. The preservation of the gel microstructure and, consequently, peptide-curcumin hydrophobic interactions during intestinal digestion could explain why curcumin release from the peptide hydrogel was lower than from the WPI gel. This work provides innovative results regarding the potential of using food-derived peptide hydrogels as an entrapment system for curcumin and its preservation during digestive conditions.

Toluidine blue O photosensitizer combined with caffeic acid improves antibacterial performance by increasing the permeability of cell membrane

Photodynamic therapy has always been an antibacterial tool for solving multi-drug resistant bacteria problem, but the side effects and the low efficiency due to the high aggregation and low solubility of photosensitizers limit its application. Due to the anti-inflammatory effect of caffeic acid, two novel photosensitizers (CA-1-TBO, CA-TBO) were synthesized by conjugating caffeic acid with toluidine blue O (TBO). The structures have been characterized by 1HNMR and high-resolution mass spectrometry. The UV-vis absorption, fluorescence spectra and the octanol-water partition coefficient of two photosensitizers were measured to evaluate their photophysical properties and hydrophilic/hydrophobic properties. Compared with parent TBO, the two modified photosensitizers have shown a higher quantum yield and kinetics constants of singlet oxygen, which has been supported by the simulation results of density functional theory. As drug-resistant representatives of gram-positive and gram-negative bacteria, respectively, S. aureus and P. aeruginosa have been used for in vitro antibacterial experiments. The sterilization efficiencies of the two modified photosensitizers far exceed that of parent TBO. The results of the octanol-water partition coefficient and fluorescence quantification showed that modified photosensitizers CA-1-TBO and CA-TBO could be more accumulated than parent TBO. Based on scanning electron microscopy images, protein gel electrophoresis, and the conductivity of the bacterial solution, the possible mechanism of improved antibacterial photodynamic efficiencies could be induced by membrane permeability due to the caffeic acid effect. The findings demonstrate the significant potential of natural phenolic compounds in the development of photosensitizer molecules with characteristics such as more efficient, biocompatible and less side effects.

Impact of heat-set and cold-set gelling polysaccharides on potato protein gelation: Gellan gum, agar, and methylcellulose

The plant-based meat market is growing due to concerns about the sustainability of the modern food system. Plant-based meats are often constructed from blends of food biopolymers, such as plant proteins and polysaccharides. This study characterizes the thermal setting properties of potato protein (10%) and polysaccharide (2 wt%) mixtures containing polysaccharides with different reversible gelling behaviors: agar (cold set); gellan gum (cold set); or methyl cellulose (heat set). Each sample was heated above the thermal denaturation temperature of the potato proteins to promote protein unfolding, aggregation, and network formation. The addition of the polysaccharides tended to increase the complex shear modulus of the biopolymer blends before heating but increase or decrease it after heating depending on polysaccharide type. The shear modulus and hardness of the gels formed after heating tended to increase after addition of the cold-set polysaccharides but decrease after the addition of the heat-set polysaccharides, especially at refrigerator temperatures. Differential scanning calorimetry data showed that the potato proteins underwent irreversible denaturation after heating for all samples. Zeta-potential analysis showed that the potato proteins and all polysaccharides were negatively charged under the pH conditions used. There was greater water loss during heating for the composite gels containing methyl cellulose, which may have been due to its increase hydrophobicity at high temperatures. Appearance and microstructure analysis showed that phase-separation occurred after mixing the polysaccharides with the potato proteins, which was attributed to a segregation mechanism. The knowledge obtained from this study may help the food industry to optimize protein-polysaccharide blends to create gels with characteristics and structures that can mimic different plant-based meat products.

Regulation of Protein Flexibility and Promoting the Cod Protein Gel Formation Using Ultrasound Treatment.

In order to obtain a soft-textured protein gel suitable for the elderly, the cod protein gel was prepared by improving the protein flexibility under ultrasound treatment. It has been found that the increase in ultrasonic power, protein flexibility, particle size, ζ-potential, surface hydrophobicity, and α-helix content of preheated cod protein exhibited an increasing trend. The improvement of protein flexibility promoted uniformity and density of the gel network, water retention, and texture properties. The flexibility of preheated cod protein increased to 0.189, the water holding capacity of the gel reached up to 99.41%, and the hardness increased to 49.12 g, as the ultrasonic power level increased to 400 W. Protein flexibility was correlated well with the cohesiveness of the gel. The storage modulus (G') initially decreased and then increased during the heating-cooling process. The attractive forces forming between the flexible protein molecules during cooling in the ultrasound treatment groups promoted protein self-assembly aggregation and formed the cod protein gel. The gel obtained at 100-400 W could be categorized as Level 6─soft and bite-sized according to the International Dysphagia Diet Standardization Initiative (IDDSI) framework, indicating that the cod protein gel has potential as an easy-to-swallow diet for the elderly.

Interactions between pea protein and gellan gum for the development of plant-based structures

Plant-based analogs have been developed to mimic foods from animal sources by using ingredients from vegetable sources. Among the strategies to produce plant-based structures is the gelation of mixtures between plant proteins and polysaccharides. In this study, our aim was to investigate gels of pea proteins and gellan gum with high protein concentration and the addition of salt (potassium and sodium chloride). In the first step, a qualitative mapping was performed to select pea protein and gellan gum concentrations to produce self-sustainable gels. After that, the effect of salt addition was investigated for the formulations containing 10–15 % (wt) pea protein and 0.5–1 % (wt) gellan gum. The results showed that the gels containing potassium ions were more rigid and less deformable, with lesser water loss by syneresis. The morphological analysis showed a spatial exclusion of pea protein from the gel network mainly structured by the gellan gum. While potassium ions led to a more compact network, calcium ions promoted higher pores in the structure. Depending on the composition, the mechanical properties of gels were similar to some products from animal sources. So, the information obtained from these gels can be applied to the structuring of formulations in the development of plant-based analogs.

Fabrication and characterization of soy protein isolation-ferulic acid antioxidant hydrogels.

Soy protein gel products are prone to direct oxidation by reactive oxygen during processing and transportation, thus reducing their functional properties and nutritional values. A covalent complex was prepared with soy protein isolate (SPI) and ferulic acid (FA) catalyzed by laccase (LC). The complex was further treated with microbial transglutaminase (TGase) to form hydrogels. The structural changes of the covalent complex (SPI-FA) and the properties and antioxidant stability of hydrogel were investigated. The SPI-FA complexes were demonstrated to be covalently bound by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and they had the least hydrophobic and free sulfhydryl groups at a 1.0 mg mL-1 FA concentration. The α-helix of complexes increased from 11.50% to 27.39%, and random coil dropped from 26.06% to 14.44%. The addition of FA caused SPI fluorescence quenching and redshift. The hydrogel was formed after the complex was induced with TGase, and its hardness and water holding capacity was increased by 50.61% and 26.21%, respectively. Scanning electron microscopy showed that a layered and ordered gel structure was formed. After in vitro digestion, the complex hydrogels maintained stable antioxidant activity, and the free radical scavenging rates of DPPH and ABTS reached 87.65% and 84.45%, respectively. SPI-FA covalent complexes were prepared under laccase catalysis, and complex hydrogels were formed by TGase. Hydrogels have stable antioxidant activity, which provides application prospects for the antioxidant development of food. © 2023 Society of Chemical Industry.

Tea polyphenol-mediated network proteins modulate the NaOH-heat induced egg white protein gelling properties

The crosslinked network aggregation of proteins regulates the formation and property maintenance of gels. In this study, we analyzed the influence of tea polyphenol (TP)-mediated network proteins on the formation and gel properties of NaOH-thermally induced egg white gels (EWGs). The free sulfhydryl content decreased slowly from 13.12 μmol/g pro to 10.89 μmol/g pro with the addition of TP and reduced the degradation of ovalbumin as a network protein during the formation of EWGs. With increased TP and NaOH concentrations, the surface hydrophobicity and absolute value of ζ-potentials of EWG improved obviously. The mechanical test results revealed that an increase in the NaOH concentration weakened the textural properties of EWG, while adding TP increased the gel strength from 161.38 g to 195.89 g, but the rupture strength decreased from 2144.6 g to 471.59 g. Rheological results demonstrated that EWG with TPs exhibited enhanced rigidity, an increased proportion of covalent bonds, and a more compact gel network structure than EWG without TPs. The stress relaxation results were fitted using the five-element Maxwell model, which revealed that an increase in the NaOH concentration decreased gel hardness and viscosity, whereas an increase in the TP concentration enhanced gel hardness. The increase in the NaOH and TP concentrations significantly increased the surface hydrophobicity of EWGs and promoted the rise of intermolecular forces and disulfide bond interactions. Heat modification further denatured and crosslinked the non-alkalized EW proteins, resulting in a compact protein gel network structure and improved gelation characteristics.

Composition of bacterial blends for fermentation-induced pea protein emulsion gels using multi-property screening of lactic acid bacteria

In this study, a comprehensive screening and identification process to pinpoint lactic acid bacteria (LAB) strains capable of enhancing gel firmness and elevating the flavor profile in pea protein-based protein gels was conducted, aiming to demonstrate how tailored starter cultures for specific applications can provide high-quality sensory attributes in fermented plant-based cheese. Thirteen single strains were selected from a poll of 90 different LAB based on their acidification performance, contribution to gel firmness, removal of off-flavors and production of dairy-associated volatile organic compounds. They were combined in 64 different blends of five strains each and screened again for the same parameters. Fast acidifying strains were prioritized for food preservation reasons to inhibit undesirable spoilage. Fermentation of pea protein emulsions with Streptococcus thermophilus, Lactobacillus, and Lactococcus blends resulted in a significant reduction in volatile organic compounds associated with beany and green off-flavor, a production of dairy-associated compounds, and satisfactorily contributed to gel firmness.

Plant Protein Heat-Induced Gels: Formation Mechanisms and Regulatory Strategies

With increasing awareness of human health, proteins from plant sources are being considered as alternatives to those from animal sources. The market for plant-based meat substitutes is expanding to satisfy the growing consumer demand. However, the functional properties of natural proteins frequently do not satisfy the needs of the modern food industry, which requires high-quality properties. Research on improving the functional properties of proteins is currently a popular topic. Based on the gel properties of proteins, this study focused on the formation mechanism of heat-induced protein gels, which will be helpful in expanding the market for plant protein gel products. Regulatory strategies for heat-induced gels were reviewed, including protein composition, pH, ionic strength, other food components, and processing techniques. The effects of other food components (such as polysaccharides, proteins, polyphenols, and liposomes) are discussed to provide insights into the properties of plant protein gels. Studies have shown that these factors can effectively improve the properties of plant protein gels. In addition, the development and application potential of emerging processing technologies that can contribute to safe and effective applications in actual food production are discussed. For the future, plant protein gels are playing an irreplaceable role in the new direction of future food.

Creation of Next-Generation Plant-Based Seafood Using Emulsion Gel Technology: Omega-3-Enriched Sea Foie Gras Analogs

Plant-based seafood analogs are gaining increasing popularity as replacements for traditional fish and other seafood products due to environmental (stock depletion, pollution, and bycatch issues) and health (bioaccumulated toxins, norovirus, and allergies) concerns associated with them. Several companies have launched plant-based fish products, but the market still lacks alternatives to shellfish and other sea delicacies. In this study, a plant-based sea foie gras (monkfish liver product) analog was developed using duckweed RuBisCO protein and omega-3-rich flaxseed oil to form emulsion gels. These gels consisted of a high concentration of flaxseed oil droplets dispersed within a gelled RuBisCO protein network. It was hypothesized that the high disperse phase volume fraction of the oil droplets and the heat-set gelation properties of the RuBisCO proteins would enable us to create emulsion gels that mimicked the properties of sea foie gras. A natural pigment (β-carotene) was incorporated into the oil phase of the emulsions to mimic the red-orange color of conventional sea foie gras. The structural, textural, and optical properties of real and plant-based sea foie gras analogs were characterized using scanning electron microscopy, confocal microscopy, dynamic shear rheology, texture profile analysis, and colorimetry. Emulsion gels prepared using 40% flaxseed oil and 10% RuBisCO proteins produced plant-based products that closely simulated the texture and color of the real products. Rheological analysis suggested that the oil droplets acted as active fillers within the protein gels. Our results suggest that emulsion gels may be used to create more sustainable and healthier plant-based seafood products.

Cell Microencapsulation Within Engineered Hyaluronan Elastin-Like Protein (HELP) Hydrogels.

Three-dimensional cell encapsulation has rendered itself a staple in the tissue engineering field. Using recombinantly engineered, biopolymer-based hydrogels to encapsulate cells is especially promising due to the enhanced control and tunability it affords. Here, we describe in detail the synthesis of our hyaluronan (i.e., hyaluronic acid) and elastin-like protein (HELP) hydrogel system. In addition to validating the efficacy of our synthetic process, we also demonstrate the modularity of the HELP system. Finally, we show that cells can be encapsulated within HELP gels over a range of stiffnesses, exhibit strong viability, and respond to stiffness cues. © 2023 Wiley Periodicals LLC. Basic Protocol 1: Elastin-like protein modification with hydrazine Basic Protocol 2: Nuclear magnetic resonance quantification of elastin-like protein modification with hydrazine Basic Protocol 3: Hyaluronic acid-benzaldehyde synthesis Basic Protocol 4: Nuclear magnetic resonance quantification of hyaluronic acid-benzaldehyde Basic Protocol 5: 3D cell encapsulation in hyaluronan elastin-like protein gels.

Mechanism for improving the gel properties of transglutaminase-mediated porcine myofibrillar protein by ultrasonic pretreatment combined with carrageenan.

To improve the limitation of transglutaminase on the quality of myofibrillar protein (MP) gel, this study investigated the synergistic effect of ultrasonic pretreatment in combination with carrageenan on the gel properties of transglutaminase-mediated MP gels. The synergistic effect generated gel with lower surface hydrophobicity and fluorescence intensity. Combined with the secondary structure results, it can be hypothesized that the synergistic effect caused the rearrangement of the proteins and the formation of aggregates wrapping hydrophobic groups, which changed the structure and phase behavior of the proteins. The synergistic effect also improved the formation of dense and interpenetrating gel networks, which reduced cooking loss and produced composite MP gels with optimal gel strength. Moreover, FTIR spectroscopy revealed the presence of electrostatic interactions in the hybrid gel system. This study provides a theoretical basis and experimental foundation for the effective use of high-tech composite functional components to improve the quality of gel products.

Insights into the in vitro digestibility of pork myofibrillar protein with different ionic polysaccharides from the perspective of gel characteristics.

In this work, the simulated gastrointestinal digestion of myofibrillar protein gels (MPGs) with anionic xanthan (XMP) and sodium alginate (SMP)/cationic chitosan (CSMP)/neutral curdlan (CMP) and konjac (KMP) was investigated to develop muscle-gelled foods with good qualities before and after eating. The results indicated that the neutral CMP and KMP groups had higher gel strength and protein digestibility than the CSMP group. Xanthan and sodium alginate facilitated myosin degradation in gastrointestinal digestion because of the weak wraps between protein and anionic polysaccharides, gaining plentiful peptides (1790 and 1692 respectively) with molecular weights below 2000Da. Chitosan and neutral curdlan could improve the strength of MP gel but inhibited proteolysis and resulted in low contents of released amino acids via the strong cross-linked network blocking trypsin contact. This work provides a theoretical basis for developing low-fat meat products with good qualities and digestion behaviors by simply controlling the ionic types of polysaccharides.