The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Elucidating the mechanisms of ultrasound treatment combined with κ-carrageenan addition enhancing the gelling properties of heat-induced myofibrillar protein gel
Abstract
This work investigated the effect of ultrasound (US) treatment synergized with κ-carrageenan (KC) on the gel properties, structural characteristics and microstructures of myofibrillar protein (MP) gel. The results demonstrated that simply adding KC enhanced the gel strength and water holding capacity (WHC) of MP gels. Moreover, the gel strength and WHC of MP gels were increased by 56.67 % and 76.19 % via 20 min US treatment synergized with KC, which was mainly attributed to the changes in sulfhydryl content, surface hydrophobicity, and fluorescence intensity of MP gels. Based on the results of molecular docking and secondary structure, it can be hypothesized that the synergistic effect resulted in the rearrangement of the proteins, which altered the interaction site between MP gels and KC, accompanied by stronger binding. Furthermore, the microstructural results indicated that moderate US treatment (20 min) facilitated the production of a more compact and denser MP gels matrix with uniformly sized and distributed pores. However, excessive US treatment (40 and 50 min) caused the MP gels to form looser and disordered gel structure, which reduced the gel strength and WHC. This study suggested that combining of US and KC was a potential tactic to enhance the gelling properties of heat-induced MP gels.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Optimized ultrasound parameters such as exposure time and intensity could regulate interaction sites between proteins and polysaccharides, strengthening binding interactions and augmenting mechanical properties.
“Optimized ultrasound parameters such as exposure time and intensity could regulate the interaction sites between proteins and polysaccharides, strengthening their binding interactions and augments mechanical properties (C. Zhao et al. 2023; S. Lin et al. 2025; S. Lin, Liang, et al. 2024).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as S. Lin, Liang, et al. 2024
Ultra-high pressure and ultrasound treatment are beneficial for formation of β-sheet in gel network.
“Ultra‐high pressure (UHP) and ultrasound treatment are beneficial for the formation of β‐sheet in the gel network (S. Lin, Liang, et al. 2024).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as S. Lin, Liang, et al. 2024
Citations
Cites
Wei, S., Liang, X., Xu, Y., Kong, B., Li, X., Zhang, H., Liu, Q., & Wang, H. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.126997 · Cited by 28
Self-citation
Flagged first, then by citations
Research works printed but not linked: 44
- Cao, 2021, Textural and gel properties of frankfurters as influenced by various κ-carrageenan incorporation methods, Meat Science, 176, 10.1016/j.meatsci.2021.108483 · DOI
- Cao, 2022, Effect of different κ-carrageenan incorporation forms on the gel properties and in vitro digestibility of frankfurters, Food Hydrocolloids, 129, 10.1016/j.foodhyd.2022.107637 · DOI
- Cao, 2023, Elucidation of interactions between myofibrillar proteins and κ-carrageenan as mediated by NaCl level: Perspectives on multiple spectroscopy and molecular docking, International Journal of Biological Macromolecules, 248, 10.1016/j.ijbiomac.2023.125903 · DOI
- Cao, 2024, Effects and mechanisms of different κ-carrageenan incorporation forms and ionic strength on the physicochemical and gelling properties of myofibrillar protein, International Journal of Biological Macromolecules, 257, 10.1016/j.ijbiomac.2023.128659 · DOI
- Chen, 2023, Structural and functional properties of self-assembled peanut protein nanoparticles prepared by ultrasonic treatment: Effects of ultrasound intensity and protein concentration, Food chemistry, 413, 10.1016/j.foodchem.2023.135626 · DOI
- Chen, 2023, Structural and physicochemical properties of the different ultrasound frequency modified Qingke protein, Ultrasonics Sonochemistry, 94, 10.1016/j.ultsonch.2023.106338 · DOI
- Chen, 2020, Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi, Journal of the Science of Food and Agriculture, 100, 2252, 10.1002/jsfa.10254 · DOI
- Feng, 2024, Effects of transglutaminase coupled with κ-carrageenan on the rheological behaviours, gel properties and microstructures of meat batters, Food Hydrocolloids, 146, 10.1016/j.foodhyd.2023.109265 · DOI
- Feng, 2024, Underlying mechanisms and combined effects of transglutaminase and κ-carrageenan on the quality profiles and in vitro digestibility of frankfurters, Food Hydrocolloids, 147, 10.1016/j.foodhyd.2023.109344 · DOI
- Gao, 2023, Design and characterization of low salt myofibrillar protein-sugar beet pectin double-crosslinked gels pretreated by ultrasound and konjac glucomannan: Conformational and gelling properties, Food Hydrocolloids, 141, 10.1016/j.foodhyd.2023.108717 · DOI
- Gao, 2021, Effect of ultrasound pre-treatment modes on gelation properties of silver carp surimi, LWT-Food Science and Technology, 111945
- Gao, 2023, Modification of low-salt myofibrillar protein using combined ultrasound pre-treatment and konjac glucomannan for improving gelling properties: Intermolecular interaction and filling effect, International Journal of Biological Macromolecules, 250, 10.1016/j.ijbiomac.2023.126195 · DOI
- Han, 2022, Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior, Ultrasonics Sonochemistry, 89, 10.1016/j.ultsonch.2022.106140 · DOI
- Han, 2023, High-intensity ultrasound combined with glycation enhances the thermal stability and in vitro digestion behaviors of myofibrillar protein aqueous solution, International Journal of Biological Macromolecules, 251, 10.1016/j.ijbiomac.2023.126301 · DOI
- Huang, 2020, Glycosylated fish gelatin emulsion: Rheological, tribological properties and its application as model coffee creamers, Food Hydrocolloids, 102
- Jia, 2022, Improved effect of flaxseed gum on the weakened gelling properties of myofibrillar protein induced by catechin, Food Chemistry, 372, 10.1016/j.foodchem.2021.131136 · DOI
- Jiang, 2020, Thermal gelling properties and structural properties of myofibrillar protein including thermo-reversible and thermo-irreversible curdlan gels, Food Chemistry, 311, 10.1016/j.foodchem.2019.126018 · DOI
- Li, 2021, Structural characteristics and emulsifying properties of myofibrillar protein-dextran conjugates induced by ultrasound maillard reaction, Ultrasonics Sonochemistry, 72, 10.1016/j.ultsonch.2020.105458 · DOI
- Li, 2022, Exploring the activation mechanism of alcalase activity with pulsed electric field treatment: Effects on enzyme activity, spatial conformation, molecular dynamics simulation and molecular docking parameters, Innovative Food Science & Emerging Technologies, 76, 10.1016/j.ifset.2022.102918 · DOI
- Li, 2023, Mechanism for improving the gel properties of transglutaminase-mediated porcine myofibrillar protein by ultrasonic pretreatment combined with carrageenan, Food Chemistry, 426, 10.1016/j.foodchem.2023.136635 · DOI
- Lin, 2024, Combined effect of ultrasound treatment and κ-carrageenan addition on the enhancement of gelling properties and rheological behavior of myofibrillar protein: An underlying mechanisms study, International Journal of Biological Macromolecules, 257, 10.1016/j.ijbiomac.2023.128569 · DOI
- Liu, 2015, Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-shifting and mild heating processes, Journal of Agricultural and Food Chemistry, 63, 4853, 10.1021/acs.jafc.5b01331 · DOI
- López-Monterrubio, 2020, Huauzontle (chenopodium nuttalliae saff.) protein: Composition, structure, physicochemical and functional properties, Food Hydrocolloids, 108, 10.1016/j.foodhyd.2020.106043 · DOI
- Lu, 2022, Physicochemical properties and microstructure of composite surimi gels: The effects of ultrasonic treatment and olive oil concentration, Ultrasonics Sonochemistry, 88, 10.1016/j.ultsonch.2022.106065 · DOI
- Nyaisaba, 2019, Effect of hydroxyl-radical on the biochemical properties and structure of myofibrillar protein from Alaska Pollock (theragra chalcogramma), LWT-Food Science & Technology, 106, 15, 10.1016/j.lwt.2019.02.045 · DOI
- Raoufi, 2019, Ultrasonic degradation of persian gum and gum tragacanth: Effect on chain conformation and molecular properties, Ultrasonics sonochemistry, 52, 311, 10.1016/j.ultsonch.2018.12.002 · DOI
- Vargas, 2020, High-intensity ultrasound pretreatment influence on whey protein isolate and its use on complex coacervation with kappa carrageenan: Evaluation of selected functional properties, Ultrasonics Sonochemistry, 70
- Wang, 2022, Structural basis for high-intensity ultrasound treatment in rheology of myofibrillar protein extracted from white croaker in relation to their solubility, LWT- Food Science and Technology, 15
- Wang, 2023, Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism, Ultrasonics Sonochemistry
- Wang, 2023, Synergistic effect of high-intensity ultrasound and pH-shifting on the functionalities of chicken wooden breast myofibrillar protein: Reveal the mechanism of protein structure change, LWT- Food Science and Technology, 181, 10.1016/j.lwt.2023.114743 · DOI
- Wei, 2023, Investigation of the effects and mechanism of incorporation of cross-linked/acetylated tapioca starches on the gel properties and in vitro digestibility of kung-wan, Meat Science, 204, 10.1016/j.meatsci.2023.109265 · DOI
- Wu, 2023, Insight into the mechanism of enhancing myofibrillar protein gel hardness by ultrasonic treatment combined with insoluble dietary fiber from oat, LWT- Food Science and Technology, 178, 10.1016/j.lwt.2023.114539 · DOI
- Xin, 2023, Improving the gel properties of salted egg white/cooked soybean protein isolate composite gels by ultrasound treatment: Study on the gelling properties and structure, Ultrasonics Sonochemistry, 97, 10.1016/j.ultsonch.2023.106442 · DOI
- Xiong, 2019, Effect of ultrasound on physicochemical properties of emulsion stabilized by fish myofibrillar protein and xanthan gum, Innovative Food Science & Emerging Technologies, 54, 225, 10.1016/j.ifset.2019.04.013 · DOI
- Xu, 2022, A structural explanation for enhanced binding behaviors between β-lactoglobulin and alkene-aldehydes upon heat- and ultrasonication-induced protein unfolding, Food Hydrocolloids, 130, 10.1016/j.foodhyd.2022.107682 · DOI
- Xu, 2023, The improvement of the oxidative oat (Avena sativa L.) protein based on ultrasound treatment: Study of structural, emulsifying, and rheological properties, Food Hydrocolloids, 144, 10.1016/j.foodhyd.2023.109047 · DOI
- Yang, 2017, Effects of ultrasound pretreatment with different frequencies and working modes on the enzymolysis and the structure characterization of rice protein, Ultrasonics Sonochemistry, 38, 19, 10.1016/j.ultsonch.2017.02.026 · DOI · Paper page
- Yang, 2023, pH and ultrasound driven structure-function relationships of soy protein hydrolysate, Innovative Food Science & Emerging Technologies, 85, 10.1016/j.ifset.2023.103324 · DOI
- Yu, 2023, Hemp seed protein and chlorogenic acid complex: Effect of ultrasound modification on its structure and functional properties, International Journal of Biological Macromolecules, 233, 10.1016/j.ijbiomac.2023.123521 · DOI
- Zhao, S. M., Li, Z., Liu, Y., Yuan, X. R., Kang, Z. L., Zhu, M. M., & Ma, H. J. (2022). High-pressure processing influences the conformation, water distribution, and gel properties of pork myofibrillar proteins containing artemisia sphaerocephala krasch gum. Food Chemistry: X, 30(6), 14, 100320. DOI: https://doi.org/10.1016/j.fochx.2022.100320. · DOI
- Zhao, 2022, Trace the difference driven by unfolding-refolding pathway of myofibrillar protein: Emphasizing the changes on structural and emulsion properties, Food Chemistry, 367
- Zhang, 2017, Effects of high intensity ultrasound modification on physicochemical property and water in myofibrillar protein gel, Ultrasonics sonochemistry, 34, 960, 10.1016/j.ultsonch.2016.08.008 · DOI
- Zhang, 2022, Effects of ultrasonic-microwave combination treatment on the physicochemical, structure and gel properties of myofibrillar protein in penaeus vannamei (litopenaeus vannamei) surimi, Ultrasonics sonochemistry, 90, 10.1016/j.ultsonch.2022.106218 · DOI
- Zheng, 2019, Effect of κ-carrageenan on gelation and gel characteristics of Antarctic krill (Euphausia superba) protein isolated with isoelectric solubilization/precipitation, Food Chemistry, 278, 644, 10.1016/j.foodchem.2018.11.080 · DOI
Cited by
Sorted by citations
Cao, C.-A., Zhang, J., Kong, B.-H., Sun, F.-D., Zhang, H.-W., & Liu, Q. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110205 · Cited by 71
Self-citationXu, W., Li, X.-Y., Wen, X.-K., Wang, Y.-B., Sun, B.-G., & Xu, D.-X. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111605 · Cited by 39
Yuan, D., Zhang, J., Zhao, Z., Kong, B.-H., Chen, J.-X., Zhang, D., Liu, Q., & Cao, C.-A. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110481 · Cited by 36
Self-citationFang, Q., Xu, T., Su, R.-H., Dai, S., Wang, J., Zhu, W., Yang, B.-W., Tong, X.-H., Wang, H., & Jiang, L.-Z. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142274 · Cited by 34
Chen, Q.-L., Guan, J., Wang, Z.-L., Wang, Y., Wang, X., & Chen, Z.-J. (2024) · Foods · doi:10.3390/foods13213413 · Cited by 33
“…polysaccharide with a negative charge from ionized carboxyl groups, This finding was consistent with the previous reports about the impacts of other anionic polysaccharides (carrageenan and gum arabic) on the surface hydrophobicity of soybean protein gel and myofibrillar protein gel [35,36].”
ResultFeng, Y.-Y., Li, X., Zhao, Z., Kong, B.-H., Cao, C.-A., Sun, F.-D., Liu, Q., & Huang, X.-N. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111253 · Cited by 25
Self-citationLi, F., Hou, H., Zhao, T., Song, G.-S., Wang, D.-L., Yuan, T.-L., Li, L., & Gong, J.-Y. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.143325 · Cited by 24
Lin, S., Li, X., Lv, H., Kong, B.-H., Cao, C.-A., Sun, F.-D., Liu, Q., & Huang, X.-N. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111234 · Cited by 22
Self-citationLin, S., Li, X., Zhang, J., Kong, B.-H., Cao, C.-A., Sun, F.-D., Zhang, H.-W., Liu, Q., & Liu, C. (2024) · Meat Science · doi:10.1016/j.meatsci.2024.109554 · Cited by 19
Self-citationDesigning Protein Gels for Nutrient Delivery: From Formulation to Digestion
Dong, X., Wang, Y., Chen, X. D., & Selomulya, C. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70424 · Cited by 17
“In a MP-k-carrageenan system, β -turn content as the predominant structure positively correlated with gel strength (S. Lin et al. 2024 ).”
Feng, Y.-Y., Sun, Z., Zhang, J., Shi, P., Kong, B.-H., Cao, C.-A., Sun, F.-D., & Liu, Q. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110693 · Cited by 17
Self-citationLi, H., Zhang, W., Nunekpeku, X., Li, C.-H., Wang, Y., Sheng, W., & Guan, B. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.146268 · Cited by 16
Yuan, D., Li, C., Zhang, J., Kong, B.-H., Sun, F.-D., Zhang, H.-W., Liu, Q., & Cao, C.-A. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137483 · Cited by 15
Self-citationLin, S., Liu, Y.-T., Li, C., Kong, B.-H., Li, M., Liu, Q., & Cao, C.-A. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112339 · Cited by 13
Self-citationLi, H., Sheng, W., Nunekpeku, X., Hu, Y., & Chen, Q.-S. (2025) · Food Control · doi:10.1016/j.foodcont.2025.111298 · Cited by 13
Chai, J., Zhang, W.-Y., Zhao, X., & Xu, X.-L. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.145227 · Cited by 12
Tian, M., Li, M.-X., Liu, X., Li, M., Song, Y.-Y., Du, J., Wang, H., Jiang, L.-Z. Z., Tian, T., & Huang, Z.-X. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2025.147800 · Cited by 11
Chai, J., Zhao, X., Zhang, W.-Y., Wang, Y., & Xu, X.-L. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c05352 · Cited by 10
Lin, S., Sun, Z., Li, C., Kong, B.-H., Cao, C.-A., Xia, X.-F., Zhang, H.-W., & Liu, Q. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110633 · Cited by 10
Self-citationLi, Q., Liu, S., Cao, Y., Cheng, Y.-J., Yan, X., Chen, J., Dai, T.-T., Shen, P.-Y., Mcclements, D., Xu, J., et al. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112118 · Cited by 9
Li, H., Sheng, W., Nunekpeku, X., Li, C., Zhang, W., & Wang, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145301 · Cited by 8
Wang, L.-M., Zhang, Y.-X., Yang, Q., Li, K., Ma, W.-C., & Bai, Y.-H. (2025) · Food Chemistry: X · doi:10.1016/j.fochx.2025.102684 · Cited by 9
“The secondary structure of PPI gel samples was determined as described by Lin et al. (2024).”
Exploring the gelation potentials of chicken heart batter: From by-product to product.
Li, M., Jiang, L., Guo, Z., Lin, J., Zheng, H., Lin, W., Zeng, H., Wu, J.-K., Lei, H., & Wu, S. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.142316 · Cited by 8
He, N., Li, T., Li, L., Zhang, X., Liu, J., Xiao, Z., Lan, M., Wang, S., Li, B., & Yuan, Y. (2026) · Food Chemistry: X · doi:10.1016/j.fochx.2026.103763 · Cited by 5
“…could be attributed to the US40-induced cavitation and turbulence, which promoted the structural unfolding of both MPs and polysaccharides, thereby intensifying their interactions and facilitating the formation of more compact gel networks (He, Zhao, et al., 2023; Lin, Liang, Zhao, et al., 2024).”
Sun, X.-C., Zhu, S.-H., Fan, C., He, D.-Q., Lin, Y., & Ye, T.-L. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.163778 · Cited by 3
Feng, Y.-Y., Liu, Y.-T., Li, C., Kong, B.-H., Chen, Q., Zhang, H.-W., & Liu, Q. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112941 · Cited by 2
Self-citationPeng, J., Shu, W., Guan, J., Xiong, S., Liu, Q.-Q., Huang, Y., Xie, Y., Yuan, Y.-J., & Dong, X. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150893 · Cited by 2
Self-citationYang, J.-J., Sha, T., Jiang, Z., Fang, M.-L., Wen, Y., & Wang, S.-G. (2026) · Langmuir · doi:10.1021/acs.langmuir.5c05521 · Cited by 2
Lin, Y.-W., Lu, J.-J., Huang, D.-W., & Huang, P.-H. (2025) · LWT · doi:10.1016/j.lwt.2025.118452 · Cited by 2
Lin, S., Li, X., Li, C., Kong, B.-H., Cao, C.-A., Sun, F.-D., Zhao, Y.-C., & Liu, Q. (2025) · Food Chemistry: X · doi:10.1016/j.fochx.2025.102814 · Cited by 2
“Challenges such as substantial cooking loss, low fat retention, and weakened gel structure are frequently encountered, and they tend to considerably reduce the nutritional value and quality of meat products (Cao et al., 2023; Lin, Liang, et al., 2024).”
Self-citationChen, J., Zhang, M., Cao, S.-M., Lin, X.-Z., Huang, Z.-J., Zang, M.-W., & Wang, D.-Y. (2026) · Food Production, Processing and Nutrition · doi:10.1186/s43014-026-00430-8 · Cited by 1
“Ultrasound-assisted technology has demonstrated promise in addressing such instability constraints (Chen et al., 2023a; Liang et al., 2024).”
InfluentialHuang, R., Fang, Y.-P., Yin, H., Zhong, Y., Lu, W., Yang, L.-N., & Deng, Y. (2026) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2026.125247 · Cited by 1
Xu, H., Huan, H., Huang, M., Gao, Z.-W., Liu, L., Cui, L.-M., Jin, Q.-Z., Wang, X.-G., & Jin, J. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112548 · Cited by 1
Lin, S., Sun, Z., Liu, Y.-T., Cao, C.-A., Kong, B.-H., Zhang, H.-W., & Liu, Q. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.147147 · Cited by 1
Self-citationUltrasound-optimised flavour system for reduced-energy milk tea
Goh, W.-D.-Y., Chong, L., Thoo, Y., Murtini, E. S., & Huda, N. (2026) · Applied Food Research · doi:10.1016/j.afres.2026.102717
Saritsiri, A., Ployleang, N., Saengsuk, N., Sonklin, C., & Phumsombat, P. (2026) · LWT · doi:10.1016/j.lwt.2026.120138
Jiang, L., Yang, F., Peng, J., Liu, D., Xie, Y., Liu, Q.-Q., & Yuan, Y.-J. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119839
Self-citationZhang, R.-Y., Hu, W., Gao, Q., Yang, Y.-J., Li, J.-H., Su, Y.-J., Gu, L.-P., & Chang, C.-H. (2026) · Journal of Food Science · doi:10.1111/1750-3841.71538
Luo, C.-B., Shi, Y.-X., Ramzan, M., Zhang, H.-D., Jia, D.-Y., Guo, L.-H., & Zhu, J. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113405
Floating Synthesis of Porous Coordination Crystals With Absorption Capability Reinforcement.
Zheng, Y.-H., Ma, Y., Zhuang, Q., Jiang, Y.-Y., Hou, N.-S., Chen, K.-J., Ruan, Y., & Wei, B. (2026) · Small · doi:10.1002/smll.75365
Zhang, X.-D., Yun, C.-J., Li, J., Zhu, L., Qi, J., & Zhang, Y.-B. (2026) · Food Research International · doi:10.1016/j.foodres.2025.118326
Influence of Yeast β‑Glucan on the Quality of Pangasius Fish Mince Balls
Anand, S., Pati, B., Mehta, N., Patel, A. B., Gaurav, K., Singh, A., Singh, N., Nath, H., Singh, B., & Priyadarshini, M. (2025) · ACS Omega · doi:10.1021/acsomega.5c09317
Metadata
- Authors
- Lin, S., Liang, X., Zhao, Z., Kong, B., Cao, C., Sun, F., & Liu, Q.
- Affiliations
- Northeast Agricultural University (CN)
- Corresponding author
- Liu, Qian
- Venue
- Food Research International
- Publisher
- Elsevier BV
- Published
- 2024-04
- Volume
- 182
- Pages
- 114177
- ISSN
- 0963-9969 (ISSN-L)
- OpenAlex
- W4392345678
- Cited by
- 44
- References
- 0
- Citations by year
- 2026: 16 · 2025: 19 · 2024: 9
- FWCI
- 12.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Research International (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Science Fund for Distinguished Young Scholars of Heilongjiang Province (JQ2021C003)
- National Natural Science Foundation of China (32172233)
- Northeast Agricultural University (NEAU2023QNLJ-014)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- ultrasound treatment, kappa-carrageenan, myofibrillar protein gels, gel strength, water holding capacity, carbohydrate-protein interactions, sulfhydryl content, surface hydrophobicity, gel microstructure, pore size distribution, molecular docking, protein secondary structure
- MeSH terms
- Carrageenan, Gels, Hot Temperature, Muscle Proteins, Rheology, Water, Molecular Docking Simulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
