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This study investigated the gelling properties, rheological behaviour, and microstructure of heat-induced, low-salt myofibrillar protein (MP) gels containing different levels (2%, 4%, 6%, and 8%, w/w) of cross-linked (CTS) or acetylated (ATS) tapioca starch. The results indicated that either CTS or ATS significantly enhanced the gel strength and water-holding capacity of low-salt MP gels (P < 0.05), an outcome verified by the rheological behaviour test results under different modes. Furthermore, iodine-staining images indicated that the MP-dominated continuous phase gradually transited to a starch-dominated phase with increasing CTS or ATS levels, and 4% was the critical point for this phase transition. In addition, hydrophobic interactions and disulphide bonds constituted the major intermolecular forces of low-salt MP gels, effectively promoting phase transition. In brief, modified tapioca starches possess considerable potential application value in low-salt meat products., Competing Interests: Declaration of competing interest The authors declared that they have no conflicts of interest to this work., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study investigated the changes in conformation and gelling properties of myofibrillar protein (MP) from Penaeus vannamei under various ultrahigh pressure (UHP)-heat assisted technologies. The results indicated that UHP heat-assisted technology enhanced the cross-linking of the gel network by causing a rearrangement of the secondary structure of MP. Microstructural analysis revealed that MP gels treated with UHP heat-assisted technology exhibited a more uniform gel network structure. Additionally, UHP heat-assisted technology improved the binding capacity of water molecules within the gel network, particularly in the two-stage UHP heat-assisted (PBH) condition at 400 MPa. Gels prepared under this condition demonstrated the highest gel strength, measuring 386.4 g·mm. Furthermore, in vitro simulated digestion showed that PBH method significantly improved the digestibility of MP gels, suggesting that the UHP heat-assisted technology had the potential to produce easily digestible MP gel-based aquatic foods., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Frozen surimi quality generally correlates with oxidation, but impacts of protein oxidation on salt-dissolved myofibrillar protein (MP) sol in surimi remain unclear. Hence, physicochemical and gelling properties of MP sol with different oxidation degrees were investigated subjected to freeze-thaw cycles. Results showed that mild oxidation (≤1 mmol/L) improved unfrozen MP gel quality with lowest cooking loss (3.29 %) and highest hardness (829.76 N). Whereas, oxidized sol suffering freeze-thawing degenerated severely, showing reduction of 23.85 % of salt soluble protein contents with H 2 O 2 concentrations of 10 mmol/L. Shearing before heating influenced gelling properties of freeze-thawed sol, depending on oxidation levels. Oxidized gel with shearing displayed disorganized network structures, whereas gel without shearing displayed relatively complete appearances without holes under high oxidation condition (10 mmol/L). Overall, freeze-thaw process aggravated denaturation extents of MP sol subjected to oxidation, further causing high water loss and yellow color of heat-induced gel, especially to gel with shearing., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study investigated the effect of ultrasound (US) combined with pre- and post-addition of κ-carrageenan (KC) on the gelling properties, structural characteristics and rheological behavior of myofibrillar proteins (MP) under low-salt conditions. The results showed that US combined with either pre- or post-addition of KC rendered higher gel strength and water holding capacity (WHC) of MP gels than those treated with US alone and added with KC alone (P < 0.05). US combined with pre-addition of KC facilitated the binding between MP and KC, which enhanced the gel strength and WHC of the mixed MP gels and significantly improved the rheological behavior of MP. This was also confirmed by the highest surface hydrophobicity, disulfide bonds and β-sheet content of the MP gels with US combined with pre-addition of KC. Moreover, microstructural results reflected a denser structure for the pre-addition of KC in combination with US. However, US combined with post-addition of KC resulted in limited MP unfolding and relatively weak hydrophobic interactions in the composite gels, which were less effective in improving the gel properties of the MP gels. This study provides potential strategies for enhancing the gelling properties of low-salt meat products via application of US and KC., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Frozen surimi sol incline to protein oxidation, but the quality control strategies based on oxidation remain limited. Hence, the antioxidant and cryoprotective effects of γ-polyglutamic acid (γ-PGA) on freeze-thawed salt-dissolved myofibrillar protein (MP) sol were investigated. Results showed that γ-PGA could effectively regulate protein oxidation of MP sol during freeze-thawing with lower carbonyl contents and less oxidative cross-linking. Meanwhile, γ-PGA primely maintained sol protein structures, showing reduction of 15.28% of salt soluble protein contents at γ-PGA addition of 0.04% under unoxidized condition. Additionally, compared to the control group without oxidation treatment, cooking loss of heat-induced gel with 0.04% γ-PGA decreased by 47.19%, while gel strength obviously increased by 57.22% respectively. Overall, moderate γ-PGA addition (0.04%) could inhibit protein oxidation of sol, further improving frozen stability of sol through hydrogen bonds and hydrophobic interaction, but excessive γ-PGA was adverse to sol quality due to severe cross-linking between γ-PGA and MP., Competing Interests: Declaration of competing interest The authors declare no conflict of interest., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study investigated the effects of ultrasound-assisted phosphorylation on gelling properties of fish gelatin (FG). Ultrasound-assisted phosphorylation (UP) for 60, 90, and 120 min resulted in >6.54% increase of phosphorylation degree and decreased zeta potential of FG. Atomic force microscopy revealed that UP-FGs showed larger aggregates than P-FGs (normal phosphorylation FGs). Low frequent-NMR and microstructure analysis revealed that phosphorylation enhanced water-binding capability of FG and improved the gel networks. However, UP60 had the highest gel strength (340 g), gelling (17.96 °C) and melting (26.54 °C) temperature while UP90 and UP120 showed slightly lower of them. FTIR analysis indicated thatβ-sheet and triple helix content increased but random coil content decreased in phosphorylated FGs. Mass spectrometry demonstrated phosphate groups mainly bound to serine, threonine and tyrosine residues of FG and UP-FG exhibited more phosphorylation sites. The study showed that mild phosphorylation (UP60) could be applied to improve FG gel properties., Competing Interests: Declaration of competing interest The authors declare that there is no any conflict of interest., (Copyright © 2024. Published by Elsevier Ltd.)

The pectin was extracted using H 2 SO 4 , HNO 3 , and HCl from the pulp of four coffee varieties (Harar, Sidama, Jimma, and Guji) collected from different regions of Ethiopia. The effect of extraction temperature, time, solid-to-liquid ratio, types of acid and coffee varieties on the physiochemical properties and yield of pectin were studied. A maximum pectin yield, which was 12.7 %, was obtained from Harar coffee pulp treated with H 2 SO 4 . The equivalent weight of the extracted pectin varied from 1111 to 1667 g/mol. The methoxyl contents of the extracted pectin ranged from 4.23 to 7.13 %. The degrees of esterification and anhydrouronic acid of the pectin ranged from 53 to 68.5 % and 35.5 to 68.8 %, respectively. The results show the yield and physiochemical properties of the coffee pulp pectin depend on extraction parameters, acid types, and coffee varieties. Moreover, the pectin extracted from coffee pulp showed strong gelling properties., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m 2 /g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the β-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate-polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)

Ulvan, a sulfated polysaccharide extracted from Ulva spp., has garnered significant attention in the food and pharmaceutical industries due to its potential health benefits. These include immunomodulation, antiviral, anti-inflammatory, anti-hyperlipidemic, and anti-cancer effects. Nonetheless, practical applications in these fields remain limited due to an incomplete understanding of its gelation mechanisms. Additionally, the underlying mechanisms of its gelation have not been completely understood and thoroughly reviewed. The primary objective is to provide current insights into ulvan's gelling mechanisms and potential health impacts. This review also delves into the existing applications of ulvan polysaccharides. By unraveling these aspects, the information provided in this work is expected to deepen our understanding of ulvan's gelation mechanisms and its prospective role in enhancing health, holding promise for advancements in the fields of food science and disease prevention. This work's theoretical insights contribute significantly to a deeper understanding of these aspects, which holds paramount importance in unleashing the full potential of ulvan and elevating its scientific significance., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Knowledge regarding the denaturation process and control methods for depolymerized sol-state myofibrillar proteins (MPs) during freezing remains scant. This study investigated the effects of protein cross-linking treatment before freezing on physicochemical and subsequent gelation properties of MPs sol subjected to freeze-thaw (F-T) cycles. Results indicated that after five F-T cycles, cross-linked MPs sols showed increased high molecular weight polymers and bound water (T 21a and T 21b ) mobility, suggesting enhanced protein-protein interactions at the expense of protein-water interactions. Upon heating after F-T cycles, gels formed from cross-linked sols exhibited significantly higher hardness, springiness, and cooking loss ( P  < 0.05), alongside more contracted gel networks. Correlation analysis revealed that the formation and properties of thermal gel after freezing closely relate to changes in molecular conformation and chemical bonds of cross-linked MPs sol during freezing. This study provides new insights into regulating the freezing stability and post-thawed thermal processing properties of sol-based surimi products., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2024 The Authors.)

This study investigated impact of high-density lipoprotein (HDL) on thermal aggregation and gelling behavior of myosin in relation to varied pHs. Results revealed that HDL modified myosin structure before and after heating, with distinct effects observed at varied pH. Under pH 5.0, both myosin and HDL-MS exhibited larger aggregates and altered microstructure; at pH 7.0 and 9.0, HDL inhibited myosin aggregation, resulting in enhanced solubility, reduced turbidity and particle size. Comparative analysis of surface hydrophobicity, free sulfhydryl groups and secondary structure highlighted distinct thermal aggregation behavior between MS and HDL-MS, with the latter showing inhibitory effects under neutral or alkaline conditions. Gelation behavior was enhanced at pH 7.0 with maximum strength, hardness, water-holding capacity and rheological properties. Under acidic pH, excessive protein aggregation resulted in increased whiteness and rough microstructure with granular aggregates. Under alkaline pH, gel network structure was weaker, possibly due to higher thermal stability of protein molecules. Scanning electron microscopy revealed expanded HDL protein particles at pH 7.0, accounting for decreased gel strength and altered rheological properties compared with myosin gel. Overall, the results indicated a positive role of HDL at varied pH in regulating thermal aggregation of myosin and further impacting heat-induced gel characteristics., Competing Interests: Declaration of competing interest The authors report there are no competing interests to declare., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The purpose of the present study was to investigate the gelling properties and in vitro digestibility of myofibrillar protein (MP) gels under low-salt condition as mediated by different concentrations of thermo-reversible curdlan gels (TRC) or thermo-irreversible curdlan gels (TIRC). The results showed that the incorporation of TRC or TIRC obviously improved the gel strength and water holding capacity of MP gels (P < 0.05). Those properties were most improved by adding 0.3 % TRC or TIRC with gel strength of 0.18 N or 0.17 N and WHC of 54.85 % or 49.05 %. Meanwhile, both TRC and TIRC promoted the transformation of α-helix into β-sheet, as well as hydrophobic interactions and disulfide bonds, which are the main forces for the maintenance of the MP gels. The microstructure revealed that the formation of dense and uniform protein network structures can be promoted by the addition of TRC or TIRC. The different modes of interaction between TRC or TIRC and MP resulted in different microstructures of the MP gels. Furthermore, incorporation of TRC or TIRC significantly reduced in vitro protein digestibility, especially for the 0.3 % (w/w) form (P < 0.05). Meanwhile, MP gels had the lowest in vitro protein digestibility after the addition of TRC (66.67 %) compared to the form of TIRC (70.93 %). Therefore, our present study indicated that incorporation form of TRC or TIRC have distinct implications on regulating the gelling properties and in vitro digestibility of MP gels under low-salt condition., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The impact of low-frequency alternating magnetic field thawing (LF-MFT) on the physicochemical and gelling properties of porcine myofibrillar proteins (MP) was studied. Results showed that compared to atmosphere thawing (AT), LF-MFT helped in inhibiting the oxidation and denaturation of protein during thawing, thereby maintaining a superior MP gel (P < 0.05). In particular, LF-MFT-4 (LF-MFT at 4 mT) could decrease the oxidation of MP, which might be due to having a higher content of total sulfhydryl and less carbonyl of MP than other thawing treatments. The denaturation of MP was reduced since LF-MFT-4 led to less aggregation and degradation than AT. The gelling properties were also retained, and a compact and homogeneous network structure was formed after LF-MFT-4, resulting in excellent water retention. These findings suggested that LF-MFT-4 improved the gelling properties of MP by inhibiting its oxidation and denaturation, demonstrating a potential application of LF-MFT in meat thawing., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

This work aimed to investigate the combined effect of ultrasound (US) treatment and κ-carrageenan (KC) addition on the gelling properties and rheological behaviors of myofibrillar protein (MP). Without US treatment, the KC incorporation promoted the gel strength and water-holding capacity (WHC) of MP gels. These properties were further improved by 20 min US treatment with gel strength of 98.61 g and WHC of 79.87 %, which was mainly attributed to changes associated with hydrophobic interactions and disulfide bonds and the transformation from α-helix to β-sheet in MP gels. In addition, US treatment for 20 min effectively resulted in a more homogeneous polymer distribution of the MP-KC mixed system, leading to lower particle size and the largest G' and G″ values of the MP-KC mixed gels. However, longer US treatment times (30, 40 and 50 min) rendered lower gel strength, WHC, storage modulus and loss modulus of MP-KC mixed gels, which was mainly due to the formation of loose and disordered gel structures. Our present results indicated that the application of US to MP for an intermediate treatment time (20 min) combined with KC provides a potential and novel strategy to promote the gel qualities of heat-induced MP gels., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

Arabinoxylans (AXs) are compounds with high nutritional value and applicability, including prebiotics or supplementary ingredients, in food manufacturing industries. Unfortunately, the recovery of AXs may require advanced separation and integrated strategies. Here, an analysis of the emerging techniques to extract AXs from cereals and their by-products is discussed. This review covers distinct methods implemented over the last 2-3 years, identifying that the type of method, extraction source, AX physicochemical properties and pre-treatment conditions are the main factors influencing the recovery yield. Alkaline extraction is among the most used methods nowadays, mostly due to its simplicity and high recovery yield. Concurrently, recovered AXs applied in food applications is timely reviewed, such as potential bread ingredient, prebiotic and as a wall material for probiotic encapsulation, in beer and non-alcoholic beverage manufacturing, complementary ingredient in bakery products and cookies, improvers in Chinese noodles, 3D food printing and designing of nanostructures for delivery platforms., Competing Interests: Declaration of competing interest The authors declare no conflict of interest., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The present work was aimed to investigate the effects of incorporating κ-carrageenan into myofibrillar protein (MP) as a dry powder (CP) or water suspension (CW) and the ionic strength (0.3 or 0.6 M sodium chloride (NaCl)) on MP physicochemical and gelling properties. The results indicated that incorporation of either CP or CW significantly increased turbidity, surface hydrophobicity, particle size and rheological behaviour of MP. In contrast, the protein solubility and fluorescence intensity of MP decreased when added with each form of κ-carrageenan (P < 0.05). These observed effects improved MP's gelling properties and produced a more compact and homogenous gel network after heating treatment. Moreover, the addition of CW rendered higher gel strength, water holding capacity and intermolecular interactions, such as ionic, hydrogen and disulphide bonds and hydrophobic interactions in MP gel compared with those added with CP, especially for 0.3 M NaCl (P < 0.05). Furthermore, addition of CW significantly decreased the α-helix content of MP gels (P < 0.05), which mainly contributing to the transformation from a random structure to an organised configuration. In addition, a higher NaCl concentration (0.6 M) enhanced the gelling properties of MP gels compared with 0.3 M NaCl concentration in the presence of each form of κ-carrageenan. Therefore, our present study indicated that incorporation form of κ-carrageenan and ionic strength have distinctive effects on regulating physicochemical characteristics and improves gelling properties of MP., Competing Interests: Declaration of competing interest The authors declared that they have no conflicts of interest to this work., (Copyright © 2023 Elsevier B.V. All rights reserved.)

Pectin is a polysaccharide mainly used in food processing industries as an emulsifier, thickener, stabilizer and in pharmaceuticals as an excipient, wall material and bio adhesive for improving delivery and efficiency. Raising demand for pectin, pushes to explore unconventional plant-based sources for the extraction of pectin. This work is aimed to explore the possibility of extracting pectin from the peel of banana varieties and to decipher the chemical and techno-functional properties. Among the varieties, Nendran, a plantain banana recorded higher pectin recovery (23.42 %), swelling power (23.10 gg -1 ), anhydrouronic acid (AUA) content (72.86 %) and emulsifying activity (46.19 %). Pectin from the banana peels exhibited the equivalent weight (g/mol) ranging from 943.40 (var. Bhimkol) to 1282.05 (var. Nendran). Morphological observations revealed that the extracted pectin has fragments with uneven sizes and inter-particle voids in the structure. Banana pectin behaved similar to commercial pectin in terms of rheological, textural and structural profiles. HPLC analysis and NMR spectra confirmed the dominance of galacturonic acid in the banana peel pectins. The study unveiled and opened up the avenues of utilizing banana peel as a complementary biomass for the extraction of pectin which could be used in different industrial applications., Competing Interests: Declaration of competing interest Paramasivam Suresh kumar reports financial support was provided by Indian Council of Agricultural Research., (Copyright © 2023. Published by Elsevier B.V.)

The influence of ultrasonic processing on the physicochemical characteristics, microstructure, and intermolecular forces of the hybrid gels obtained by heating the mixtures of different ratios of salted ovalbumin (SOVA)-cooked soybean protein isolate (CSPI) was investigated. With the growth of SOVA addition, ζ-potential in absolute value, cohesiveness, water-holding capacity (WHC), surface hydrophobicity, and the content of soluble protein of the hybrid gels decreased ( P  < 0.05), while the hardness, T 2 relaxation time of the hybrid gels increased ( P  < 0.05). And the compactness of the network structure of the hybrid gel increased with the increase of SOVA addition. After being treated with ultrasound, significant increases ( P  < 0.05) of ζ-potential in absolute value, cohesiveness, WHC, and surface hydrophobicity of the hybrid gels were observed. In general, ultrasonic processing is one of the effective means to improve the gel properties of SOVA-CSPI hybrid gels., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2024 The Authors.)

This study investigated the effects of ultra-high pressure (UHP) at different levels on the physicochemical properties, gelling properties, and in vitro digestion characteristics of myofibrillar protein (MP) in Tai Lake whitebait. The α-helix gradually unfolded and transformed into β-sheet as the pressure increased from 0 to 400 MPa. In addition, the elastic modulus (G') and viscous modulus (G'') of the 400 MPa-treated MP samples increased by 4.8 and 3.8 times, respectively, compared with the control group. The gel properties of the MP also increased significantly after UHP treatment, e.g., the gel strength increased by a 4.8-fold when the pressure reached 400 Mpa, compared with the control group. The results of in vitro simulated digestion showed that the 400 MPa-treated MP gel samples showed a 1.8-fold increase in digestibility and a 69.6 % decrease in digestible particle size compared with the control group., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2023 The Authors. Published by Elsevier Ltd.)

In this study, κ-carrageenan(κC) and Transglutaminase (TG) were used to modify fish gelatin (FG). Three types of modified gelatin groups FG-κC, FG-TG and FG-κC-TG were prepared. The results showed that the gel strength and textural properties of FG gels were greatly enhanced by κC modification and κC-TG complex modification, whilst pure TG modification weakened the gelling properties. And the pure 0.1 % κC modified FG had the highest gel strength and hardness, respectively. Rheological behavior showed that the complex modified FG samples had the highest viscosity, gelling points, melting points and G'∞. Fourier infrared spectra and LF-NMR analysis showed that κC and κC-TG modification respectively improved the contents of hydrogen and isopeptide that decreased the water mobility but stabilized the helical structure of gelatin gels. Fluorescence intensity showed that three types of modification decreased fluorescence intensity. While, the formation of aggregates and denser gel networks decreased in vitro digestibility of FG., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

Preserved egg white (PEW) has excellent gelling properties but is susceptible to the freshness of raw eggs. In this study, the correlation between the comprehensive freshness index (CFI) of raw eggs and the gelling properties of alkali-induced egg white gel (EWG) was elucidated. Results showed that the CFI, established by a principal component analysis (PCA) and stepwise regression analysis (SRA) methods, can be used to predict the freshness of duck eggs under storage conditions of 25 °C and 4 °C. A correlation analysis demonstrated that the CFI showed a strong negative correlation with the hardness and chewiness of alkali-induced EWG and a strong positive correlation with resilience within 12 days of storage at 25 °C and 20 days at 4 °C ( p < 0.01). It might be due to the decrease in α-helix and disulfide bonds, as well as the hydrophobic interactions showing a first decrease and then an increase within the tested days. This study can provide an important theoretical basis for preserved egg pickling.

Background: Fish gelatin (FG) has multifunctional properties similar to mammalian gelatin (MG), and it has been recognized as the optimal alternative to MG. While its poor surface-active and gelling properties significantly limit its application values, glycosylation has been successfully used to increase surface-active properties of FG, but the influence of ultrasonic-associated glycosylation (UAG) on the gelling and structural characteristics of FG is still rarely reported. This article explores UAG (100-200 W, 0.5-1 h) with κ-carrageenan (κC) on the functional properties (emulsifying, gelling and rheological properties) and structural characteristics of FG., Results: The longer time and higher power of ultrasonics accelerated the glycosylation reaction with an increase in glycosylation degree and browning index values. Compared with original FG, FG-κC mixture and bovine gelatin, UAG-modified FG possessed higher emulsification activity index, emulsion stability index, gel strength, hardness and melting temperature values. Among them, gelatin modified by appropriate ultrasonic conditions (200 W, 0.5 h) had the highest emulsifying and gelling properties. Rheological results showed that UAG contributed to the gelation process of gelatin with advanced gelation time and endowed it with high viscosity. Structural analysis indicated that UAG promoted κC to link with FG by the formation of covalent and hydrogen bonds, restricting more bound and immobilized water in the gels, exhibiting higher gelling properties., Conclusion: This work showed that UAG with κC is a promising method to produce high gelling and emulsifying properties of FG that could replace MG. © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

Background: The reduction of protein oxidation is important for maintaining the product quality of reconstituted meat. In this study, the dose-dependent effects of lentinan (LNT) on gelling properties and chemical changes in oxidatively stressed goose myofibrillar protein were investigated., Results: Myofibrillar protein (MP) with 200 μmol g -1 protein LNT increased gel strength by 87.90 ± 9.26% in comparison with LNT-free myofibrillar protein after oxidation. Scanning electron microscopy analysis revealed that the gel network containing LNT was compact, with small pores and uniform distribution. The absolute value of the zeta potential reduced significantly following oxidation of LNT with 200 μmol g -1 protein at 4 °C for 12 h compared with the zeta potential without LNT, according to the laser particle size analyzer. The incorporation of LNT increased protein solubility and -SH content, inhibited carbonyl formation, enhanced α-helix content and tryptophan intrinsic fluorescence intensity, and reduced exposure of hydrophobic groups and protein aggregation., Conclusion: The results indicated that adding LNT to myofibrillar protein could improve gel. This is related to its protective effect on conformational changes in the oxidation system. Lentinan is therefore recommended for oxidatively stressed goose meat processing to enhance the MP gelling potential. © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

In this paper, the effects of different modification orders of microbial transglutaminase (MTGase) and contents of pectin (0.1-0.5%, w / v ) on the gelling and structural properties of fish gelatin (FG) and the modification mechanism were studied. The results showed that the addition of pectin could overcome the phenomenon of high-MTGase-induced lower gelling strength of gelatin gels. At a low pectin content, the modification sequences had non-significant influence on the gelling properties of modified FG, but at a higher pectin content (0.5%, w / v ), P 0.5% -FG-TG had higher gel strength (751.99 ± 10.9 g) and hardness (14.91 ± 0.33 N) values than those of TG-FG-P 0.5% (687.67 ± 20.98 g, 12.18 ± 0.45 N). Rheology analysis showed that the addition of pectin normally improved the gelation points and melting points of FG. The structural results showed that the fluorescence intensity of FG was decreased with the increase in pectin concentration. Fourier transform infrared spectroscopy analysis indicated that the MTGase and pectin complex modifications could influence the secondary structure of FG, but the influenced mechanisms were different. FG was firstly modified by MTGase, and then pectin (P-FG-TG) had the higher gelling and stability properties.

In this study, we investigated the effects of different high-intensity ultrasound (HIU) pretreatment times (0-60 min) on the structure of β-conglycinin (7S) and the structural and functional properties of 7S gels induced by transglutaminase (TGase). Analysis of 7S conformation revealed that 30 min HIU pretreatment significantly induced the unfolding of the 7S structure, with the smallest particle size (97.59 nm), the highest surface hydrophobicity (51.42), and the lowering and raising of the content of the α-helix and β-sheet, respectively. Gel solubility showed that HIU facilitated the formation of ε-(γ-glutamyl)lysine isopeptide bonds, which maintain the stability and integrity of the gel network. The SEM revealed that the three-dimensional network structure of the gel at 30 min exhibited filamentous and homogeneous properties. Among them, the gel strength and water-holding capacity were approximately 1.54 and 1.23 times higher than those of the untreated 7S gels, respectively. The 7S gel obtained the highest thermal denaturation temperature (89.39 °C), G', and G″, and the lowest tan δ. Correlation analysis demonstrated that the gel functional properties were negatively correlated with particle size and the α-helix, while positively with Ho and β-sheet. By contrast, gels without sonication or with excessive pretreatment showed a large pore size and inhomogeneous gel network, and poor properties. These results will provide a theoretical basis for the optimization of HIU pretreatment conditions during TGase-induced 7S gel formation, to improve gelling properties., Competing Interests: The authors declare no conflict of interests.

There is an emerging consumption of the Antarctic krill (AK) muscle-based food due to its excellent nutritional value and enormous biomass storage capacity. However, the coarse texture of the muscle and the weak gelling properties of AK protein impede its expansion in surimi-based products. This investigation successfully prepared heat-induced gels of AK surimi with desirable textural properties by including Litopenaeus vannamei in varying proportions. Higher concentrations of L. vannamei resulted in improved three-dimensional printability, greater water-holding capacity (WHC), larger viscoelastic modulus, and a well-formed microstructural matrix of AK surimi, due to an increased level of myofibrillar protein. Compared with AK, L. vannamei muscle had double the salt-soluble protein content, which was corroborated by increased intensity of bands of actin, paramyosin, tropomyosin, and myosin light chains on reducing SDS-PAGE. DSC results indicated that a high ratio of L. vannamei elevated the denaturation temperature and enthalpy of myosin, sarcoplasmic protein, and actin, suggesting a high degree of cross-linking. It was also found that when hydroxypropyl cassava starch was added at 0.5% (w/w), WHC and gel strength were further improved with a more compact gel matrix. The successful preparation of unwashed mixed surimi with AK meat fully exploited in this study provides an option for AK surimi-based product industrialization., (© 2023 Wiley Periodicals LLC.)

Effects of the incorporation of ultrasound with varied intensities (0-800 W) into the thermal-induced gelation process on the gelling properties of myofibrillar protein (MP) were explored. In comparison with single heating, ultrasound-assisted heating (<600 W) led to significant increases in gel strength (up to 17.9%) and water holding capacity (up to 32.7%). Moreover, moderate ultrasound treatment was conducive to the fabrication of compact and homogenous gel networks with small pores, which could effectively impair the fluidity of water and allow redundant water to be entrapped within the gel network. Electrophoresis revealed that the incorporation of ultrasound into the gelation process facilitated more proteins to get involved in the development of gel network. With the intensified ultrasound power, α-helix in the gels lowered pronouncedly with a simultaneous increment of β-sheet, β-turn, and random coil. Furthermore, hydrophobic interactions and disulfide bonds were reinforced by the ultrasound treatment, which was in support of the construction of preeminent MP gels., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 The Author(s). Published by Elsevier B.V. All rights reserved.)

Silver carp ( Hypophthalmichthys molitrix ) is a potential source for making surimi products. However, it has the disadvantages of bony structures, high level of cathepsines and muddy off-odor which is mainly caused by geosmin (GEO) and 2-methylisoborneol (MIB). These disadvantages make the conventional water washing process of surimi inefficient (low protein recovery rate, and high residual muddy off-odor). Thus, the effect of the pH-shifting process (acid-isolating process and alkali-isolating process) on the cathepsins activity, GEO content, MIB content, and gelling properties of the isolated proteins ( IPs ) was investigated, comparing it with surimi obtained through the conventional cold water washing process (WM). The alkali-isolating process greatly boosted the protein recovery rate from 28.8% to 40.9% ( p < 0.05). In addition, it removed 84% GEO and 90% MIB. The acid-isolating process removed about 77% GEO and 83% MIB. The acid-isolated protein (AC) displayed the lowest elastic modulus (G'), the highest TCA-peptide content (90.89 ± 4.65 mg/g) and the highest cathepsin L activity (65.43 ± 4.91 U/g). The AC modori (60 °C for 30 min) gel also demonstrated the lowest breaking force (226.2 ± 19.5 g) and breaking deformation (8.3 ± 0.4 mm), indicating that proteolysis caused by the cathepsin deteriorated the gel quality of AC. The setting (40 °C for 30 min) considerably increased the breaking force (386.4 ± 15.7 g) and breaking deformation (11.6 ± 0.2 mm) of the gel made from the alkali-isolated protein (AK) ( p < 0.05). In AC and AK gel, a clearly visible cross-linking protein band with a molecular weight greater than MHC was seen, demonstrating the presence of endogenous trans-glutaminase (TGase) activity, that improved the gel quality of AK. In conclusion, the alkali-isolating process was an effective alternative method for making water-washed surimi from silver carp.

Starch-stabilized Pickering emulsions were employed as a novel particulate filler in myofibrillar protein (MP)-based gels for improving the gelling characteristics. The role of emulsions prepared by native starches (NS) with distinctive crystalline types (i.e., A-type waxy corn starch, B-type potato starch, and C-type pea starch) and their OSA-modified counterparts (A-OS, B-OS, C-OS) in the gelling performance was evaluated and compared with MP-stabilized-emulsion. Compared with MP-emulsion, starch-emulsion caused substantial increases in the gelling properties, notably for OSA-starch emulsions. Herein, A-OS exhibited up to 1.26-, 5.3-, and 2.9-fold increments in storage modulus, gel strength, and water holding capacity relative to pure MP gel, respectively, higher than B-OS and C-OS. Moreover, light microscopy evinced a more compact gel network filled with smaller and uniform oil droplets when A-OS emulsions were incorporated into the gels. The addition of OSA-starch emulsions, especially A-OS emulsion, facilitated the protein conformational conversion from α-helix to β-sheet and caused a marked reduction of free sulfhydryls in the gels; yet, the chemical forces that stabilized the gels altered, where remarkable reinforcements in hydrogen bond and hydrophobic interaction were detected, in support of the construction of splendid MP gels. Hence, OSA-starch emulsions show promise as functional components in meat products., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022. Published by Elsevier Ltd.)

Background: The contribution and mechanism of κ-/ι-carrageenan (CG) with different hydration characteristics on the gelling properties of shrimp myofibrillar protein (MP) gelation was studied., Results: The gel strength, water-holding capacity and viscoelastic properties of MP gels were significantly enhanced by 1.0% κ-/ι-CG (P < 0.05), but the microstructure showed that excessive carrageenan caused fragmentation of the gel network and a corresponding decrease in gel properties. Compared to MP-ιCG, MP-κCG showed larger breaking force and shorter breaking distance, thus enhancing the hardness and brittleness of the gel, which might be ascribed to a reinforced network skeleton and a tighter binding of κCG-myosin. However, MP-ιCG stabilized more moisture in the gel network, thereby improving the tenderness of the gel, which might be related to the electrostatic repulsion observed between the sulfate groups of ιCG and the myosin observed by molecular docking. In addition, the β-sheet content and intermolecular interactions might be positively correlated with gel properties., Conclusion: In this study, a composite gel system was constructed based on the interaction of MP and CG. The quality differences of two kinds of CG-MP gels were clarified, which will provide guidance for the application of different kinds of carrageenan and the development of recombinant meat products with specific quality. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

The present study investigated the effects of genipin cross-linking on the gelling properties of ginkgo seed protein isolate (GSPI). Cross-linking of GSPI was achieved with different concentrations (0, 0.05, 0.1, 0.2, 0.4, 0.6% w/v) of genipin at pH 6.0. Compared to pure GSPI, genipin treatment led to lower solubility, surface hydrophobicity, and fluorescence intensity, while promoted protein aggregation. Cross-linked GSPI gels exhibited markedly improved gelling properties and water holding capacity (WHC), with up to 2.1-fold increases in gel hardness and 1.3-fold increases in WHC over non-treated GSPI gel. Electrophoresis and Fourier-transform infrared spectroscopy confirmed the cross-linking. Moreover, microstructural examination showed that cross-linking with genipin resulted in protein aggregation and more porous gel matrix. Overall, genipin cross-linking demonstrated great potential for the enhancement of gelling properties of ginkgo seed protein. The current research may expand the utilization of ginkgo seeds in food applications., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

β-glucan from cereals such as wheat, barley, oats and rye are a water-soluble dietary fiber, which are composed of repeating (1→4)-β-bond β-D-glucopyranosyl units and a single (1→3)-β-D-bond separated unit. β-glucan has a series of physicochemical properties (such as viscosity, gelling properties, solubility, etc. ), which can be used as a food gel and fat substitute. Its structure endows the healthy functions, including anti-oxidative stress, lowering blood glucose and serum cholesterol, regulating metabolic syndrome and exerting gut immunity via gut microbiota. Due to their unique structural properties and efficacy, cereal β-glucan are not only applied in food substrates in the food industry, but also in food coatings and packaging. This article reviewed the applications of cereal β-glucan in hydrogels, aerogels, intelligent packaging systems and targeted delivery carriers in recent years. Cereal β-glucan in edible film and gel packaging applications are becoming more diversified and intelligent in recent years. Those advances provide a potential solution based on cereal β-glucan as biodegradable substances for immune regulation delivery system and intelligent gelling material in the biomedicine field.

The roles of panda bean protein amyloid fibrils (PDPF) in modifying the textural and rheological properties of heat-induced pea protein isolate (PPI) gels were investigated. It was found that the incorporation of PDPF significantly enhanced (p < 0.05) the strength of PPI gel. This effect was PDPF concentration-dependent and was predominantly attributable to the enhanced intermolecular interactions between PDPF and PPI through hydrogen bonds and hydrophobic interactions. Synchronously, the non-network proteins content in PPI-PDPF gels decreased from 23.6 % to 6.6 % when PDPF concentration increased from 0 to 1.50 % (w/w). Cryo-scanning electron microscopy proved that PDPF was filled in the PPI gel network leading to more compact and interconnected gel structure. However, the water holding capacity and secondary structures of PPI gel were not significantly affected. The findings of this study showed that PDPF was effective in improving the PPI gel functional quality, which provided scientific support for PDPF as a promising gel ingredient in food industrial applications., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Myofibrillar protein (MP) system with different dissociation degrees of actomyosin was constructed by addition of ATP and the effects of actomyosin dissociation on the physicochemical and gelling properties of MP sol during freeze-thaw cycles were investigated. The results showed that the salt soluble protein content of the dissociated sample with 5 mM ATP (5-pH 6.2 group) was lower than that of other groups under unfrozen state, while the fluorescence intensity and hardness of all dissociated groups were significantly lower (P＜0.05) than that of the control group. After five freeze-thaw cycles, the low-field nuclear magnetic resonance (LF NMR) revealed that the immobile water (T 22b ) in MP sol with 5 mM ATP (pH 6.9) has lower fluidity compared with the control group. In addition, rheological studies revealed that the G' (storage modulus) value at 90℃ of MP sol with 5 mM ATP (pH 6.9) showed less decrease than that of the other groups after five freeze-thaw cycles. Meanwhile, after five freeze-thaw cycles, scanning electron microscope (SEM) showed that the gel of the control group has large holes and rough structure, while the microstructure of sample with 5 mM ATP (pH 6.9) was more compact and uniform. The heat-induced gel of 5-pH 6.9 group had highest hardness and lowest cooking loss among the groups after five freeze-thaw cycles. Briefly, the dissociation of actomyosin before freezing could slow down the rate of MP denaturation and improve the gelling properties after freeze-thaw cycle., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Background: Washing is an essential process in surimi production, from which a large amount of wastewater is generated. Due to the increasing pressure of environmental protection, it is an urgent technical requirement for surimi manufacturers to reduce water usage while maintaining the quality of surimi. In this study, composition, structure and gelling properties of grass carp surimi prepared with a modified washing process (MWP) were investigated. Intermediate dehydration with various compression ratios were utilized between two washing cycles., Results: Water usage and wastewater discharge were reduced significantly by 33% and 38%, respectively, when MWP was applied. As the compression ratio increased, composition of fat, cathepsins, transglutaminase and heme proteins in surimi decreased gradually. Yield, protein content and the major protein pattern of surimi were not changed, but surface hydrophobicity gradually decreased. As the compression rate increased to 1:2.0, textural values and water holding capacity of the corresponding surimi gel decreased gradually, while whiteness increased and then remained unchanged. At a higher compression ratio (>1:1.5), aggregated network and excessive free water were observed in the surimi gel. Composition and gelling properties of the MWP surimi with a compression ratio of 1:1.2-1:1.5 were equal to those of the surimi prepared under conventional three-cycle washing., Conclusion: Results indicated that MWP demonstrated its great potential in surimi production by dramatically reducing the usage of cold water and discharge of wastewater without scarifying surimi quality. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

Emulsion gels are structured emulsion systems that behave as soft solid-like materials. Emulsion gels are commonly used in food-product design both as fat replacers and as delivery carriers of bioactive compounds. Different plant-derived proteins like soy, chia, and oat have been used in emulsion gel formulation to substitute fat in meat products and to deliver some vegetable dyes or extracts. Quinoa protein isolates have been scarcely applied in emulsion gel formulation although they seem to be a promising alternative as emulsion stabilizers. Quinoa protein isolates have a high protein content with a well-balanced amino acid profile and show good emulsifying and gelling capabilities. Unlike quinoa starch, quinoa protein isolates do not require any chemical modification before being used. The present article reviews the state of the art in food emulsion gels stabilized with vegetable proteins and highlights the potential uses of quinoa proteins in emulsion gel formulation., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Proteins are natural amphiphilic polymers that often have good emulsifying, gelling, and structure forming properties. Consequently, they can be used to assemble protein-based colloidal delivery systems for bioactive agents, such as nanoemulsions, protein nanoparticles, or microgels. However, the functional performance of some proteins is limited because of their poor water-solubility, a tendency to aggregate, and or low surface activity, which limits their application for this purpose. Therefore, physicochemical modification is often necessary to improve their technofunctional characteristics. High-intensity ultrasound (HIU) is a non-thermal processing method that has considerable potential for the modification of the structural, physicochemical, and functional properties of proteins. In this article, we review the impact of sonication on the properties of proteins, including their size, charge, surface hydrophobicity, flexibility, solubility, free sulfhydryl groups, and disulfide bond formation. In addition, the influence of sonication on the emulsifying, foaming, gelling, and encapsulation properties of proteins is reviewed. Previous studies show that high-intensity ultrasound treatments have a strong influence on the molecular characteristics of proteins (increasing their solubility, flexibility, and functionality), which improves their ability to form colloidal delivery systems., Competing Interests: Declaration of Competing Interest None., (Copyright © 2022. Published by Elsevier B.V.)

The consumption of plant proteins is increasing worldwide. These proteins have an important role in human nutrition as well as in the technological properties of foods. Thus, there is a great interest in exploring new sources of plant proteins, such as macauba (Acrocomia aculeata), which is a promising tropical palm tree, native to Brazil, whose fruits are rich in oil, proteins and dietary fiber. Hence, the objective of this work was to obtain and evaluate the physico-chemical and techno-functional properties of the macauba kernel protein isolate (MKPI). Defatted macauba kernel flour was obtained and used to produce the MKPI by isoelectric precipitation. Then, the proximate composition, amino acid profile, and physico-chemical and techno-functional properties of the MKPI were determined. The MKPI stood out for its high protein content (94.9%) and high levels of arginine (16.21%) and glutamate (20.84%). The MKPI average isoelectric point was at pH 4.9 and its proteins showed low solubility in the pH range from 4.0 to 6.0. Moreover, the hydrophobicity of MKPI proteins was higher at pH 3.5 than at pH 7.0, and they had higher oil holding capacity (153.77%) than water holding capacity (97.29%). Regarding the MKPI emulsifying and gelling properties, emulsions with 0.5% and 1.0% of MKPI remained stable during storage and the minimum gelling concentration was 14%. Thus, the MKPI has a great potential to be produced and used by the food industry due to its nutritional and techno-functional properties., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

The effects of high-intensity ultrasound on the physicochemical and gelling properties of Litopenaeus vannamei (L. vannamei) myofibrillar protein (MP) were investigated. MP solutions were subjected to ultrasound treatment (power 100 W, 300 W, and 500 W). It was found that the carbonyl and free amino contents of MP increased significantly with increasing ultrasound power, accompanied by enhanced emulsification properties. The increase of free radical and carbonyl content indicated that ultrasound induced the oxidation of MP. With the increase of ultrasound power, it was found that the total sulfhydryl content of the shrimp MP decreased, but the surface hydrophobicity increased significantly, which might be closely related to the conformational changes of MP. Meanwhile, a significant increase of β-sheet but a decrease of α-helix in the secondary structure of MP was observed with increasing ultrasound power, indicating that ultrasound treatment induced the stretching and flexibility of MP molecules. SDS-PAGE showed that L. vannamei MP consisted of myosin heavy chain, actin, myosin light chain, paramyosin and tropomyosin. Ultrasound treatment could lead to some degree of oxidative aggregation of MP. The results of rheological properties indicated that ultrasound treatment enhanced the viscoelasticity of MP and further improved the gel strength of MP gel. This study can provide a theoretical basis for the functional modification of shrimp MP and the processing of its surimi products., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 The Author(s). Published by Elsevier B.V. All rights reserved.)

Plasma is a new technology used to modify myofibrillar proteins (MPs) structure and promote protein aggregation. In order to study the mechanism of plasma modifying MPs thus the effects on qualities of MP gels, MPs were extracted by 0.6 M NaCl solution prepared with plasma-activated water (PAW) at different treatment time (0 s, 30 s, 60 s, 120 s, 240 s). With the prolonged PAW treatment time from 0 to 240 s, the pH values of natural MP solutions decreased significantly from 5.91 to 2.61 ( P  < 0.05), the H 2 O 2 concentration in PAW increased from 0 to 70.82 μg/L ( P  < 0.05), and the net negative charges of MPs first decreased and then increased ( P  < 0.05). In addition, PAW caused significantly ( P  < 0.05) weakened ionic bonds and enhanced hydrophobic interactions, which promoted the aggregation and gelation of MPs thus forming MP gel with higher gel strength and a denser three-dimensional network. Furthermore, Raman spectra and intrinsic fluorescence suggested that PAW promoted the unfolding of MP structures and transformation from α-helixes and random coils to β-sheets and β-turns. Dynamic rheology indicated a gradually increased storage modulus and shortened degradation time of MPs with an increasing treatment time of PAW. Furthermore, PAW modification significantly improved the water holding capacity of MPs gels. These results demonstrated that the declined pH of MP solutions induced by PAW and increased H 2 O 2 in PAW altered the ζ-potential of MP solutions and promoted the unfolding and aggregation of MPs during heating via hydrophobic interactions, ultimately enhancing gelling properties of MPs. The present work suggested the potential use of PAW in preparing freshwater MP gels with high quality., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2022 The Authors.)

H. illucens, black soldier fly larvae (BSFL) is one of the sustainable sources of protein. However, the research on the functionality of BSFL proteins is limited and need to be explored to increase consumer acceptance. The aim of this study is to create a gel system from BSFL protein and evaluate the impact of ultrasound treatment at different exposure time (5, 15, 30 min) on the physicochemical properties of BSFL protein. The highest values for surface hydrophobicity, size, ζ-potential were obtained after 15 min of ultrasound treatment and the same was found for the elastic modulus. Finally, confocal laser scanning microscopy (CLSM) along with image analysis revealed the lowest pore size after 15 min of treatment. The high protein content of BSFL protein extract and its promising gel system herein created, are important features to be considered for further development of insect-based food., (Copyright © 2022 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

The high-moisture extrusion of proteins from plant and animal sources should be a new way for developing alternative protein products with meat-like texture. The protein gelling properties are considered an important factor for the meat-like texture formation during the high-moisture extrusion processing. In this study, the mixed protein gelling properties from soy protein isolate (SPI) and surimi at different ratios (90:10, 80:20, 70:30, 60:40 and 50:50) were investigated to relate to the high-moisture (70%) extruding product textural properties, correspondingly. Results showed that at SPI-surimi ratio 60:40, the heat-induced gelation time was clearly extended and the gel strength became much weaker. During the high-moisture extrusion processing, at SPI-surimi ratio 80:20, the extrudate showed the higher hardness, chewiness, gel strength and fibrous degree, while excessive surimi (more than 40%) in the blends would hinder the fibrous-oriented structure formation. It suggested that SPI may act as the continuous phase that is dispersed by surimi during the high-moisture extrusion processing. Interestingly, it was found that the gel strength of SPI-surimi blends was nonlinearly correlated with the specific mechanical energy (SME) and product textural properties. The study would be helpful for improving the textural properties of alternative protein products from soy and surimi.

The present work investigated the effects of water bath heating coupled with different ultrasound treatments on the gel properties, protein conformation, microstructures and chemical interactions of silver carp surimi at low/high salt levels. Results showed that the gel strength, hardness, springiness and water holding capacity (WHC) of surimi gels at low salt concentration were inferior to those at high salt content, regardless of the treatments. Compared with the traditional water bath heating, ultrasonic-assisted treatments significantly improved the gelation properties of surimi at the same salt level. In fact, ultrasound treatment also facilitated the unfolding of α-helix structure of the protein, with the resulting exposure of internal groups further enhancing hydrophobic interactions and hydrogen bonds between protein molecules, thereby leading to the formation of denser microstructures with smaller holes. Furthermore, the most noteworthy ultrasonic treatment group was ultrasound-assisted preheating (U + W) group, whose gelation performance under low salt condition, was comparable with that of the traditional two-stage heating (W + W) group with high salt content. Overall, ultrasound-assisted water bath preheating proved to be a feasible approach to improve the gel properties and microstructures of low-salt surimi gels., (Copyright © 2022 The Author(s). Published by Elsevier B.V. All rights reserved.)

Carboxymethyl chitosan (CMCh) is an ampholytic chitosan derivative that manifests versatile applications in food industry, such as antibacterial ingredients and nutritional additives. However, its use as a cryoprotectant remains under-researched. In this study, the cryoprotective effect of CMCh oligosaccharide (CMCO) on frozen surimi (silver carp) was systematically investigated in terms of protein structures, gelling behaviors, and sensory qualities. CMCO (0.6%) was incorporated in the surimi before frozen storage (-18 °C for 60 days) while the commercial cryoprotectant (4% sucrose, 4% sorbitol) was used as a positive control. Results indicated that CMCO could inhibit the freezing-induced denaturation of myofibrillar protein, whose values of solubility, Ca 2+ -ATPase and sulfhydryl content were 24.8%, 64.7%, and 17.1% higher than the nonprotected sample, respectively, while the surface hydrophobicity was 21.6% lower. Accordingly, CMCO stabilized microstructure of the surimi gels associated with improved gel strength, viscoelasticity, water-holding capacities, and whiteness. Moreover, the cryoprotective effect of CMCO with higher degree of carboxymethyl substitution (DS: 1.2) was more pronounced than that of low-DS-CMCO (DS: 0.8). Frozen surimi treated with high-DS-CMCO achieved competitive gelling properties and sensory acceptability to those with the commercial counterpart. This study provided scientific insights into the development of ampholytic oligosaccharides as food cryoprotectants.

Effects of high internal phase emulsion (HIPE) stabilized by egg yolk-modified starch complex on the gelling properties of chicken gels with or without sodium chloride (NaCl)/sodium tripolyphosphate (TP) were studied. The addition of 30 % HIPE increased the hardness from 376 g to 590 g. The NaCl addition further improved textural and viscoelastic properties compared with the gels without NaCl. 30 % HIPE-filled gels with salts (NaCl and TP) has the highest hardness (3562 g) and the lowest cooking loss (3.41 %). Fourier transform infrared spectra (FTIR) revealed that salts, especially TP, could promote the transition of α-helices to β-sheets structure. Moreover, the chicken gels with TP had higher acyl chain disorder. In summary, the co-addition of HIPE and salt (NaCl/TP) has a positive effect on the formation of chicken gel, thereby providing potential applications in comminuted meat products., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

The effects of different salt additions (1.0%, 1.5%, 2.0%, 2.5%, 3.0%, and 3.5%) on the gelling properties and protein phosphorylation of the mixed gels (MG) formed by silver carp ( Hypophthalmichthys molitrix ) surimi with 10% crabmeat were investigated. The MG's breaking force, deformation, gel strength, and water-holding capacity (WHC) increased as the salt concentration increased. The intrinsic fluorescence intensity of the samples initially decreased and then increased, reaching the lowest when the NaCl concentration was 2.5%. The result of SDS-polyacrylamide gel electrophoresis indicated that large aggregates were formed by protein-protein interaction in the MG containing 2.5% or 3.0% NaCl, decreasing the protein band intensity. It was also found that with the addition of NaCl, the phosphorus content initially increased and then decreased, reaching the maximum when the NaCl concentration was 2% or 2.5%, which was similar to the changing trend of actin band intensity reported in the results of Western blot. These results revealed that the amount of salt used had a significant effect on the degree of phosphorylation of the MG protein. The increase in phosphorylation was linked to improved gelling properties, which could lead to new ideas for manufacturing low-salt surimi products in the future.

The mechanism between food gelation and its digestibility has attracted increasing attention over the past few decades. This study aimed to evaluate the effect of glycation degree on the gelation and digestibility of egg white gel (EWG) using an in vitro model and a multi-scale characterization of gel structure. Results showed that EWG glycated with increasing d-ribose by covalent bonds exhibited better gelling properties and lower in vitro digestibility according to the appearance of soluble proteins and peptides. Besides, glycation preference for ovotransferrin at lysine might be important for regulating gel structure and proteolysis accessibility via the ratio of fibrous and granular aggregates. Moreover, gel structure was predominant over amino acids modification for digestibility. Binding disorder and steric hindrance could ascribe to the lower digestibility of gels. These findings are enlightening for the formulation and production of food matrix with controlled digestibility through glycation in food and related pharmaceutical fields., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Fish gelatin (FG) has been extensively studied as a potential substitute for mammal gelatin. However, FG often requires different modification methods to change its physical and chemical properties due to its low gelling properties. Here, γ-polyglutamic acid (γ-PGA) and microbial transglutaminase (MTGase) were combined to modify FG to improve its gelling properties. The γ-PGA at 0.04% (w/v) and MTGase of different concentrations (0.02-0.08%, w/v) were used to modify FG, and the effects of complex modification on the gelling properties and structure of FG were studied. When the MTGase content was 0.08% (w/v), FG had the best gelling properties. In addition, the complex modification of MTGase and γ-PGA hindered the formation of the triple helix during the FG gel process. This reduced the gel rate, but significantly increased its viscosity. A schematic model was also proposed to illustrate the complex modifications of FG by MTGase and γ-PGA., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Background: Dry heat processing remains the most promising and simple approach for achieving better gelling properties of spray-dried egg white powder (EWP). Water mobility and intermolecular interactions in gels derived from EWP were investigated after subjecting EWP to various dry heating times (0-21 days)., Results: The gel hardness and water-holding capacity significantly increased with an increase in dry heating time (P < 0.05), and both parameters were positively correlated with gel transparency. In contrast to the coarser structure of untreated EWP gel, the gel of EWP corresponding to 15 days of dry heating time had a fine-stranded and orderly network structure with smaller pores. An increase in the binding force between the gel and water was observed with an increase in dry heating time due to the formation of more 'protein-water' hydrogen bonds. Increasing the dry heating time resulted in an increase in the contribution of disulfide bonds, which in turn made a significant contribution to the rigidity of the EWP gels. By contrast, a decrease in the contribution of ionic bonds and hydrophobic interactions upon increasing the dry heating time promoted the formation of orderly networks., Conclusions: Overall, gel corresponding to EWP dry heating for 15 days had better gel properties, the highest transparency and water-holding capacity, as well as a fine-stranded and orderly network structure. These results provide more information on improvement of the gel properties of EWP through dry heat treatment. © 2020 Society of Chemical Industry., (© 2020 Society of Chemical Industry.)

The effects of γ-polyglutamic aid (γ-PGA) on the gelling properties and non-covalent interactions of fish gelatin were investigated. The gel strength and melting temperature of fish gelatin gradually increased, with increasing γ-PGA concentration, although there was no significant change when the γ-PGA concentration was greater than 0.04%. As the concentration of γ-PGA increased, the electrostatic interaction of fish gelatin increased and the hydrophobic interaction between gelatin molecules decreased. The fish gelatin system was comprised of γ-PGA concentrations of 0.04 and 0.06% showing a strong hydrogen bond. When the γ-PGA concentration increased from 0 to 0.04%, more phenolic hydroxyl groups in the tyrosine residue tended to form hydrogen bonds with the protein. However, an additional increase in γ-PGA concentration to 0.1% led to enhanced hydrogen bonding with water molecules. The results of this study showed that hydrogen bonds played an important role in improving the gelling properties of gelatin by γ-PGA., (© 2019 Wiley Periodicals, Inc.)