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1.
Int J Biol Macromol ; : 134161, 2024 Jul 24.
Article in English | MEDLINE | ID: mdl-39059535

ABSTRACT

This study investigated the influence of curdlan on the gel properties of whey protein isolate (WPI). Results demonstrated that curdlan significantly improved the water-holding capacity, gel strength and rheological properties of the WPI gels. Moreover, it promoted the unfolding of the molecular structures of WPI, which was manifested by the transition from α-helix to ß-sheet, an increase in free sulfhydryl content and a decrease in surface hydrophobicity. Furthermore, 4 % curdlan promoted the formation of WPI with uniform and compact elastic gel network structures, primarily attributed to disulphide bonds, hydrogen bonds and hydrophobic interactions. However, when the addition of curdlan exceeds 4 %, excessive entanglement of curdlan chains and steric hindrance effects hinder the unfolding and folding of protein structures, weaken their interaction, result in a loose network structure and affect the gel properties. In conclusion, this study demonstrates that curdlan can effectively improve the gelling properties of WPI, suggesting its potential application in low-calorie gel-based dairy products.

2.
Food Chem ; 459: 140403, 2024 Jul 14.
Article in English | MEDLINE | ID: mdl-39024873

ABSTRACT

Ionic strength plays a significant role in the aggregation behavior of myofibrillar proteins. The study investigated the effects of KCl or CaCl2 as substitutes for NaCl on the gel properties and taste of shrimp surimi at a constant ionic strength (IS = 0.51). Increased KCl substitution ratio resulted in a reduction in α-helix content and an increase in ß-sheet content of myofibrillar proteins, thereby enhancing water holding capacity. Optimal KCl substitutions (1.5% NaCl +1.94% KCl) contributed to maintaining the desired taste and improving gel properties. CaCl2 facilitates the extraction and dissolution of myofibrillar proteins, resulting in an organized and dense gel network with significant water-holding capacity. However, excessive additions (>1.27%) resulted in a notable decrease in taste and gel strength due to excessive aggregation and precipitation of myofibrillar proteins. These findings provide a solid theoretical foundation for production of high-quality, low-salt shrimp surimi.

3.
Food Chem ; 459: 140412, 2024 Jul 17.
Article in English | MEDLINE | ID: mdl-39024885

ABSTRACT

In this study, the comprehensive quality characteristics and proteome changes of snakehead (Channa argus) surimi gel under different atmospheric cold plasma (ACP) treatment times were systematically analyzed and compared. The results showed that the ubiquitin-associated proteins and heat shock proteins were activated after ACP treatment for 90 s (ACP90), thus inducing rearrangement of surimi structural proteins. Meanwhile, the increased hydrophobic interactions and disulfide bonds might strengthen the interactions among the myofibrillar protein, keratin, and type-I collagen, which led to the formation of a dense gel network. Moreover, the high nodality between actin and myosin promoted the regulation of muscle contraction by changing the spatial obstruction of their binding sites. These beneficial effects obviously contributed to the superior water-holding capacity (76.13%), gel strength (285.6 g·cm) and viscoelasticity of snakehead surimi in the ACP90 group. These results would provide some useful information for the in-depth and efficient processing of surimi products.

4.
Int J Biol Macromol ; 276(Pt 2): 133949, 2024 Jul 16.
Article in English | MEDLINE | ID: mdl-39025172

ABSTRACT

Different methods of starch modification have been proposed to broaden its application. In this study, the effects of ternary mixtures of natural crosslinking agents: chitosan-betaine-vanillin and gelatin-betaine-vanillin on the properties of pea starch were explored. These combinations of substances were selected because they have complementary crosslinking mechanisms. The effects of the ternary crosslinker mixtures on the gelatinization, mechanical properties, thermal stability, and microstructure of pea starch were compared. Both combinations of crosslinkers enhanced the gelatinization viscosity, viscoelasticity, gel hardness, and thermal stability of the pea starch, by an amount that depended on the ratio of the different components in the ternary mixtures. In all cases, the crystal structure of the starch granules disappeared after gelatinization. The modified starch had a more compact and uniform microstructure than the non-modified version, especially when it was crosslinked by vanillin, gelatin, and betaine. The improvement in the gelation properties of the starch were primarily attributed to hydrogen bonding, electrostatic attraction, and Schiff base crosslinking of the various components present. Gelatin enhanced the gel strength more than chitosan, which was probably because of greater hydrogen bonding. Our findings suggest that the properties of starch can be enhanced by adding ternary mixtures of natural crosslinkers.

5.
Polymers (Basel) ; 16(14)2024 Jul 10.
Article in English | MEDLINE | ID: mdl-39065294

ABSTRACT

Pectin is widely used in the food and pharmaceutical industries. However, data on sweet potato pectin extraction and structural property analyses are lacking. Here, for the high-value utilization of agricultural processing waste, sweet potato residue, a byproduct of sweet potato starch processing, was used as raw material. Ammonium oxalate, trisodium citrate, disodium hydrogen phosphate, hydrochloric acid and citric acid were used as extractants for the pectin constituents, among which ammonium oxalate had a high extraction rate of sweet potato pectin, low ash content and high molecular weight. Structural and gelation analyses were conducted on ammonium oxalate-extracted purified sweet potato pectin (AMOP). Analyses showed that AMOP is a rhamnogalacturonan-I-type pectin, with a molecular weight of 192.5 kg/mol. Chemical titration and infrared spectroscopy analysis confirmed that AMOP is a low-ester pectin, and scanning electron and atomic force microscopy demonstrated its linear molecular structure. Gelation studies have revealed that Ca2+ is the key factor for gel formation, and that sucrose significantly enhanced gel hardness. The highest AMOP gel hardness was observed at pH 4, with a Ca2+ concentration of 30 mg/g, pectin concentration of 2%, and sucrose concentration of 40%, reaching 128.87 g. These results provide a foundation for sweet potato pectin production and applications.

6.
J Food Sci ; 89(7): 4298-4311, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38957101

ABSTRACT

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


Subject(s)
Glutens , Lysine , Microwaves , Triticum , Lysine/chemistry , Triticum/chemistry , Glutens/chemistry , Protein Aggregates , Plant Proteins/chemistry , Hot Temperature , Gels/chemistry
7.
Gels ; 10(7)2024 Jul 04.
Article in English | MEDLINE | ID: mdl-39057466

ABSTRACT

The network formed by wax precipitation at low temperature and colloid asphaltene at high temperature leads to poor fluidity of heavy oil, and the gelling characteristics of crude oil lead to pipeline blockage, which affects the exploitation, transportation and refining of crude oil. This work prepares a series of cationic surfactant-modified nano hydrotalcite (CSNH) to weaken the network structure and enhance the fluidity of the crude oil by the interaction of organic and inorganic functional groups on the CSNH surface and the components of the crude oil. The results show that CSNHs can all reduce the viscosity of crude oil from different oilfields, among which BTNH can reduce the viscosity of Yanglou (YL) crude oil by 98.8% (31 °C) and depress the pour point by 16.0 °C at most. In the investigation of the universality of crude oil, the modified hydrotalcite was applied to the mixed crude oil (CQH) of Changqing Oilfield, the crude oil (J76) of Jidong Oilfield, the high pour point oil (GN) of Huabei Oilfield, and the crude oil (HQ) of Tuha Oilfield. The viscosity reduction rates were 53.2%, 86.2%, 42.7%, and 63.8%, respectively. The characterization of this nano material confirms the modification of quaternary ammonium cationic surfactant on the surface, resulting in a smaller particle size, and the nano particles are stable under conventional conditions. The mechanism of viscosity and pour point reduction in crude oil by BTNH was discussed by DSC and optical microscopy analysis. The OH- and long-chain alkyl groups on the BTNH surface may interact with the resins, asphaltene and wax through hydrogen bonding and co-crystal, weakening or dispersing their aggregates, thereby improving the fluidity of crude oil. Finally, a cost evaluation was conducted on BTNH, providing useful support for subsequent promotion and application.

8.
Food Res Int ; 188: 114461, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38823861

ABSTRACT

Myofibrillar proteins are crucial for gel formation in processed meat products such as sausages and meat patties. Freeze-thaw cycles can alter protein properties, impacting gel stability and product quality. This study aims to investigate the potential of thawed drip and its membrane-separated components as potential antifreeze agents to retard denaturation, oxidation and gel deterioration of myofibrillar proteins during freezing-thawing cycles of pork patties. The thawed drip and its membrane-separated components of > 10 kDa and < 10 kDa, along with deionized water, were added to minced pork at 10 % mass fraction and subjected to increasing freeze-thaw cycles. Results showed that the addition of thawed drip and its membrane separation components inhibited denaturation and structural changes of myofibrillar proteins, evidenced by reduced surface hydrophobicity and carbonyl content, increased free sulfhydryl groups, protein solubility and α-helix, as compared to the deionized water group. Correspondingly, improved gel properties including water-holding capacity, textural parameters and denser network structure were observed with the addition of thawed drip and its membrane separation components. Denaturation and oxidation of myofibrillar proteins were positively correlated with gel deterioration during freezing-thawing cycles. We here propose a role of thawed drip and its membrane separation components as cryoprotectants against myofibrillar protein gel deterioration during freeze-thawing cycles.


Subject(s)
Freezing , Gels , Muscle Proteins , Myofibrils , Animals , Gels/chemistry , Swine , Muscle Proteins/chemistry , Myofibrils/chemistry , Food Handling/methods , Protein Denaturation , Meat Products/analysis , Hydrophobic and Hydrophilic Interactions , Solubility , Water/chemistry , Oxidation-Reduction
9.
Gels ; 10(6)2024 May 28.
Article in English | MEDLINE | ID: mdl-38920921

ABSTRACT

Silver Carp (SC) is an under-utilized, invasive species in North American river systems. In this study, the synergistic effects of manufactured Microfiber (MMF), Transglutaminase (TG), and chicken skin collagen (CLG)) to enhance surimi gel quality from frozen SC were studied. The gel strength, textural properties, rheological properties, water-holding capacity (WHC), water mobility, microstructure, and protein composition of the gel samples were determined to assess the impact of the additives individually and synergistically. The results suggested that TG had the most pronounced effect on the surimi gel properties by promoting protein cross-linking. Synergistic effects between TG, MMF, and CLG can bring effective gel property enhancement larger than the individual effect of each additive alone. With the established response-surface models, the combination of CLG and MMF can be optimized to produce surimi gels with less TG but comparable in properties to that of the optimal result with high TG usage. The findings of this study provided a technical foundation for making high-quality surimi gel products out of frozen-stored SC with synergistic utilization of additives, which could serve as guidelines for the industrial development of new surimi products.

10.
J Food Sci ; 89(7): 4079-4092, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38847743

ABSTRACT

Ohmic heating (OH) at different conditions (voltage: 15, 20, 25 V; frequency: 1, 5, 10 kHz) and one-step water bath (WB) were used to heat wash and unwash surimi prepared from fresh pre-rigor common carp. The optimal heating conditions were established through assessments of gel strength, Texture Profile Analysis (TPA), water-holding capacity (WHC), whiteness, and sensory evaluation. Then, the impact of heating modes on gelation properties of unwashed surimi based on the optimal heating conditions was investigated. The study findings indicated a significant enhancement in gel properties compared to WB. Unwashed surimi gel properties showed improvement when derived from freshly caught raw fish and subjected to OH treatment. Moreover, variations in frequencies and voltages were observed to influence the heating rate. Optimal gel quality was achieved at 10 kHz 20 V (10 V/cm), facilitating swift progression through the gel deterioration stage, inhibition of protein hydrolyzing enzymes activity, and establishment of a stable gel network. Continuing to increase the heating rate would disrupt its network structure, resulting in diminished gel strength and WHC. The best quality of unwashed surimi gel was achieved by heating to 40°C for 30 min, followed by heating to 90°C for another 30 min (40°C 30 min + 90°C 30 min) under 10 kHz 20 V. The gel strength increased when held for 1 h at 40°C. For optimal heating efficiency, the heating mode of 40°C 30 min + 90°C 30 min is recommended to prepare unwashed surimi gel. PRACTICAL APPLICATION: Ohmic heating, as a rapid food heat treatment method, can both increase the heating rate and improve the gelation properties of freshwater surimi. There is a wide range of potential applications for the heat treatment of the surimi.


Subject(s)
Carps , Fish Products , Food Handling , Gels , Hot Temperature , Animals , Gels/chemistry , Fish Products/analysis , Food Handling/methods , Humans , Taste , Cooking/methods , Heating/methods , Water/chemistry
11.
Food Chem ; 455: 139841, 2024 Oct 15.
Article in English | MEDLINE | ID: mdl-38824724

ABSTRACT

Microcrystalline cellulose was modified by TEMPO oxidation combined with ultrasound to prepare modified cellulose-based emulsion. The effect of different emulsion concentration on gel properties and protein conformation of surimi was investigated. The results showed the length and width of microcrystalline cellulose were reduced, and a large amount of -COOH was introduced into modified cellulose. Direct addition of flaxseed oil decreased the gel strength and WHC from 3640.49 g·mm and 76.94% to 2702.95 g·mm and 75.89%, respectively, while 5% modified cellulose-based emulsion could improve the gel properties of surimi. Surimi gel containing 5% emulsion had the highest hydrophobic interaction, disulfide bond and ß-sheet content. Moreover, protein network structure was the densest in 5% emulsion group. Therefore, modified cellulose-based emulsion could be used to compensating for the negative impact of direct addition of flaxseed oil on surimi, which provided a new idea for the development of healthy and new emulsified surimi products.


Subject(s)
Cellulose , Emulsions , Fish Products , Gels , Cellulose/chemistry , Emulsions/chemistry , Animals , Gels/chemistry , Fish Products/analysis , Protein Conformation , Fish Proteins/chemistry , Hydrophobic and Hydrophilic Interactions
12.
Food Chem ; 455: 139870, 2024 Oct 15.
Article in English | MEDLINE | ID: mdl-38850985

ABSTRACT

The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 â†’ 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues. The amount of soluble proteins in hybrids generally increased with salt concentrations and PPI substitution. While muscle proteins (mixed Sarc and Myof) had the strongest gelling capacity, hybrid proteins also exhibited moderate aggregation and gelling activity based on the sol→gel rheological transition and gel hardness testing. Sarc and pea 7S/11S globulins collectively compensated for the attenuated gelling capacity of mixed proteins due to diminishing Myof in the hybrids. Immobilized water within hybrid protein gels was tightly bonded (T2 from nuclear magnetic resonance), consistent with the dense and uniform microstructure observed. These findings offer a new knowledge base for developing reduced-salt hybrid meat analogues.


Subject(s)
Gels , Muscle Proteins , Pea Proteins , Gels/chemistry , Muscle Proteins/chemistry , Animals , Pea Proteins/chemistry , Rheology , Meat Products/analysis , Sodium Chloride/chemistry , Pisum sativum/chemistry , Meat Substitutes
13.
Food Chem X ; 22: 101451, 2024 Jun 30.
Article in English | MEDLINE | ID: mdl-38803671

ABSTRACT

This study aimed to extract sturgeon oil (SO) from the sturgeon head and apply it to sturgeon meat to produce surimi gel. The effects of SO and its Pickering emulsion on the qualities of surimi gel were investigated. The results demonstrated that Pickering emulsions improved the quality deterioration of the gel caused by the direct addition of SO, especially the soy isolate protein (SPI) emulsion and the pea isolate protein (PPI) emulsion. Pickering emulsions contributed to a more uniform and compact network structure of the gel, improved the texture properties, enhanced the freeze-thaw stability, and reduced lipid oxidation. Additionally, compared to the addition of exogenous lipids such as peanut oil and linseed oil, SO and its Pickering emulsion better maintained the characteristic flavor of sturgeon surimi gel. This study provides valuable data and feasible ideas for expanding the utilization of sturgeon by-products and developing new types of surimi gel products.

14.
Foods ; 13(10)2024 May 08.
Article in English | MEDLINE | ID: mdl-38790747

ABSTRACT

This study aimed to investigate the effect of Gnaphalium affine extract (GAE) (0.04, 0.2 and 1 mg/g protein) on the gel properties of porcine myofibrillar proteins (MPs) in a simulated Fenton oxidation system, using tea polyphenols (TPs) at similar concentrations of 0.04, 0.2, and 1 mg/g protein, respectively, as a contrast. The findings revealed that as the TP concentration increased, the water retention of MP gels decreased significantly (p < 0.05). In contrast, MP gels containing medium and high concentrations of GAE exhibited significantly higher water retention than those with low concentrations of GAE (p < 0.05). When the concentration of GAE was increased to 1 mg/g protein, the strength of MP gels was significantly reduced (p < 0.05) by 33.32% compared with the oxidized control group, suggesting that low and medium GAE concentrations support MP gel formation. A texture profile analysis indicated that an appropriate GAE concentration improved gel structure and texture. Dynamic rheological characterization revealed that low concentrations of TP (0.04 mg/g protein) and low and medium concentrations of GAE (0.04 and 0.2 mg/g protein) strengthened the protein gel system. Conversely, high concentrations of TP and GAE (1.0 mg/g protein) damaged the protein gel system or even promoted the collapse of the gel system. Scanning electron microscopy revealed that higher TP concentrations disrupted the gel, whereas low and medium GAE concentrations maintained a more continuous and complete gel network structure compared with the oxidized control group. This indicates that an appropriate GAE concentration could effectively hinder the destruction of the gel network structure by oxidation. Therefore, based on the obtained results, 0.2 mg/g protein is recommended as the ideal concentration of GAE to be used in actual meat processing to regulate the oxidization and gel properties of meat products.

15.
Int J Biol Macromol ; 269(Pt 1): 132114, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38714279

ABSTRACT

Mesona chinensis polysaccharide (MCP) has excellent gel-forming characteristic, previous studies showed that MCP could affect the gelling and structural properties of rice starch, but the effect of MCP on rice starch from different types is not clarified. In this study, the effects of MCP on the pasting, rheological, and structural characteristics of glutinous rice starch (GRS), japonica rice starch (JRS), and indica rice starch (IRS) were investigated. The results showed that GRS-MCP has the best viscosity, its peak and final viscosities are higher than JRS-MCP and IRS-MCP. The gel network structure was enhanced by MCP in the order of IRS > JRS > GRS, which was reflected by greater elasticity, higher gel strength and hardness, and less free water in JRS-MCP and IRS-MCP. MCP also enhanced the ordered structure and thermal stability of the three starch gels, which is conducive to their application in the market. These findings provide new theoretical insights to produce rice starch-based foods.


Subject(s)
Gels , Oryza , Polysaccharides , Rheology , Starch , Oryza/chemistry , Starch/chemistry , Polysaccharides/chemistry , Gels/chemistry , Viscosity , Lamiaceae/chemistry , Water/chemistry
16.
Int J Biol Macromol ; 270(Pt 2): 132262, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38734356

ABSTRACT

Exopolysaccharide produced by lactic acid bacteria has various functions. In the present study, one anti-oxidant polysaccharide fraction, namely S1-EPS, was extracted and purified from Pediococcus acidilactici S1, and its structure and its potential effect on the gel properties of fat substitute meat mince were investigated. The results showed that S1-EPS, one of homogeneous polysaccharides, was mainly composed of Gal, Glc, and Man in molar ratio of 7.61: 15.25: 77.13 and molecular weight of 46.975 kDa. The backbone of EPS-S1 contained →2,6)-α-D-Manp-(1→,→2)-α-D-Manp-(1→,→3)-α-D-Glcp-(1 → and a small amount of→6)-ß-D-Manp-(1→. The linkages of branches in EPS-S1 were mainly composed of α-D-Manp-(1→ attached to a sugar residue →2,6)-α-D-Manp-(1→O-2 or ß-D-Galp-(1→ attached to a sugar residue →2,6)-α-D-Manp-(1→O-6. Furthermore, as S1-EPS increased, the meat minced gel pores decreased, and the surface became smooth. A remarkable inhibitory effect on the lipid oxidation of meat minced gel was found as S1-EPS concentration increased. Overall, S1-EPS was found to have substantial potential in low-fat meat products by serving as a natural, anti-oxidant, and functional additive.


Subject(s)
Fat Substitutes , Pediococcus acidilactici , Polysaccharides, Bacterial , Polysaccharides, Bacterial/chemistry , Pediococcus acidilactici/metabolism , Pediococcus acidilactici/chemistry , Fat Substitutes/chemistry , Molecular Weight , Antioxidants/chemistry , Antioxidants/pharmacology , Gels/chemistry , Meat Products/microbiology
17.
Int J Biol Macromol ; 271(Pt 2): 132701, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38810856

ABSTRACT

In this study, we investigated the effects of various low-frequency ultrasound-assisted extraction processes, including ultrasound-assisted acid-soaked water bath extraction (UAW), ultrasound-assisted water bath extraction after acid soaking (AUW), acid-soaked water bath extraction followed by ultrasonics (AWU), and acid-soaked water bath extraction without ultrasound (CON), on the structural properties, thermal stability, gel properties, and microstructure of sheep's hoof gelatin. The results revealed that the primary components of sheep's hoof gelatin consisted of α1-chain, α2-chain (100-135 kDa), and ß-chain. In addition, it was observed that among the three sonication groups, sheep's hoof gelatin extracted in the AUW group exhibited the highest yield (27.16 ± 0.41 %), the best gel strength (378.55 ± 7.34 g), and higher viscosity at the same shear rate. The gelling temperature (25.38 ± 0.45 °C) and melting temperature (32.28 ± 0.52 °C) of sheep's hoof gelatin in the AUW group were significantly higher than those in the other groups (p > 0.05). Moreover, our experiments revealed that the sequence of low-frequency ultrasonic pretreatment processes was a crucial factor influencing the gel properties and structural characteristics of sheep's hoof gelatin. Specifically, the acid treatment followed by the ultrasound-assisted approach in the AUW group yielded high-quality and high-yield sheep's hoof gelatin.


Subject(s)
Gelatin , Gels , Animals , Gelatin/chemistry , Sheep , Gels/chemistry , Viscosity , Temperature , Ultrasonic Waves , Sonication/methods
18.
J Dairy Sci ; 2024 May 16.
Article in English | MEDLINE | ID: mdl-38762104

ABSTRACT

Milk fan cheese, a type of stretched -cheese, presents challenges in its stretch-forming. This study investigated the impacts of complex phosphates (sodium tripolyphosphate and sodium dihydrogen phosphate, STPP-DSP) on the gelling properties of acid-induced milk fan gel and the mechanisms contributing to its stretch-forming. The treatment of milk fan gel with STPP-DSP resulted in improved functional and textural properties compared with the control group. In particular, drawing length increased significantly from 69.67 nm to 80.33 nm, and adhesiveness increased from 1737.89 g/mm to 1969.79 g/mm. The addition of STPP-DSP also led to increased viscosity, elastic modulus (G'), and viscous modulus (G"). Microstructural analysis revealed the formation of a fibrous structure within the gel after STPP-DSP treatment, facilitating uniform embedding of fat globules and emulsification. Structural analysis showed that the addition of STPP-DSP increased ß-fold and decreased random coiling of the gel, facilitating the unfolding of protein structures. Additionally, UV absorption spectroscopy and excitation-emission matrix spectroscopy results indicated the formation of a chelate between STPP-DSP and milk fan gel, increasing protein-protein molecular interactions. Evidence from differential scanning calorimetry and x-ray diffraction demonstrated the formation of sodium caseinate chelate. Fourier transform infrared spectroscopy and zeta potential analysis revealed that the sodium caseinate chelate formed through hydrophobicity, hydrogen bonding, and electrostatic forces. These findings provided theoretical insights into how phosphates can improve the stretch-forming of milk fan gel, facilitating the application of phosphate additives in stretched -cheese processing.

19.
Food Chem X ; 22: 101405, 2024 Jun 30.
Article in English | MEDLINE | ID: mdl-38694543

ABSTRACT

This study investigated the effect of inulin with different polymerization degrees (DP), including L-inulin (DP 2-6), M-inulin (DP 10-23) and H-inulin (DP 23-46), on the structural and gelation properties of potato protein isolate (PPI). Results revealed that textural properties (hardness, cohesiveness, springiness and chewiness) and water-holding capacity (WHC) of PPI-inulin composite gels were positively correlated with the inulin DP and addition content at 0-1.5% (w/v), but deteriorated at 2% due to phase separation. The addition of 1.5% H-inulin showed the most significant increment effects on the WHC (18.65%) and hardness (2.84 N) of PPI gel. Furthermore, M-/H-inulin were more effective in increasing the whiteness and surface hydrophobicity, as well as in strengthening hydrogen bonds and hydrophobic interactions than L-inulin. Fourier transform infrared spectroscopy analysis and microstructural observation indicated that inulin with higher DP promoted more generation of ß-sheet structures, and leading to the formation of stronger and finer network structures.

20.
Gels ; 10(5)2024 Apr 28.
Article in English | MEDLINE | ID: mdl-38786218

ABSTRACT

Plant proteins have the advantages of low cost and high yield, but they are still not comparable to animal proteins in processing due to factors such as gelation and solubility. How to enhance the processing performance of plant proteins by simple and green modification means has become a hot research topic nowadays. Based on the above problems, we studied the effect of gel induction on its properties. In this study, a pea protein-zein complex was prepared by the pH cycle method, and the effects of different induced gel methods on the gel properties of the complex protein were studied. The conclusions are as follows: All three gel induction methods can make the complex protein form a gel system, among which the gel strength of heat treatment and the TG enzyme-inducted group is the highest (372.84 g). Through the observation of the gel microstructure, the gel double network structure disappears and the structure becomes denser, which leads to a stronger water-binding state of the gel sample in the collaborative treatment group. In the simulated digestion experiment, heat treatment and enzyme-induced samples showed the best slow-release effect. This study provides a new method for the preparation of multi-vegetable protein gels and lays a theoretical foundation for their application in food processing.

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