The DOI matches its Crossref record; 72 of the 72 references it cites were found in a registry or an index.
Analysis of structural, functional properties and interaction mechanism of soy protein gel induced by high-performance microbial transglutaminase
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?
Microbial TG is widely used as an enzymatic modifier to reinforce covalent crosslinking between protein molecules, thereby regulating both gel properties and digestive behavior.
“Microbial TG is widely used as an enzymatic modifier to reinforce covalent crosslinking between protein molecules, thereby regulating both gel properties and digestive behavior”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Deng et al. 2025
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
HDOCK: a web server for protein–protein and protein–DNA/RNA docking based on a hybrid strategy
Yan, Y., Zhang, D., Zhou, P., Li, B., & Huang, S. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx407 · Cited by 1,479
Recent Developments and Applications of the MMPBSA Method
Wang, C., Greene, D., Xiao, L., Qi, R., & Luo, R. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00087 · Cited by 679
Properties and applications of microbial transglutaminase
Yokoyama, K.-I., Nio, N., & Kikuchi, Y. (2004) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1539-5 · Cited by 608
Park, H., Bradley, P. H., Greisen, P. J., Liu, Y., Mulligan, V. K., Kim, D. E., Baker, D. A., & DiMaio, F. (2016) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.6b00819 · Cited by 564
Protein Binding Pocket Dynamics
Stank, A., Kokh, D. B., Fuller, J. C., & Wade, R. C. (2016) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00516 · Cited by 462
Dai, S., Lian, Z., Qi, W., Chen, Y., Tong, X.-H., Tian, T., Lyu, B., Wang, M.-M., Wang, H., & Jiang, L.-Z. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.132507 · Cited by 351
Protein aggregation – Mechanisms, detection, and control
Wang, W., & Roberts, C. J. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.08.043 · Cited by 328
A nontoxic pain killer designed by modeling of pathological receptor conformations
Spahn, V., Vecchio, G. D., Łabuz, D., Rodríguez‐Gaztelumendi, A., Massaly, N., Temp, J., Durmaz, V., Sabri, P., Reidelbach, M., Machelska, H., et al. (2017) · Science · doi:10.1126/science.aai8636 · Cited by 232
Qin, X.-S., Luo, S., Cai, J., Zhong, X., Jiang, S., Zhao, Y., & Zheng, Z. X. (2016) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2016.02.010 · Cited by 214
Hua, Y., Cui, S. W., Wang, Q., Mine, Y., & Poysa, V. W. (2005) · Food Research International · doi:10.1016/j.foodres.2004.10.006 · Cited by 165
Transglutaminase factor XIII uses proteinase‐like catalytic triad to crosslink macromolecules
Pedersen, L. C., Yee, V. C., Bishop, P. D., Trong, I. L., Teller, D. C., & Stenkamp, R. E. (1994) · Protein Science · doi:10.1002/pro.5560030720 · Cited by 137
Zhang, M., Yang, Y., & Acevedo, N. C. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126421 · Cited by 130
Pravda, L., Berka, K., Vařeková, R. S., Sehnal, D., Banáš, P., Laskowski, R. A., Koča, J., & Otyepka, M. (2014) · BMC Bioinformatics · doi:10.1186/s12859-014-0379-x · Cited by 124
Effects of high intensity ultrasound on acid-induced gelation properties of whey protein gel
Shen, X., Zhao, C., & Guo, M. (2017) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2017.05.039 · Cited by 121
de la Barca, A. M. C., Ruiz‐Salazar, R. A., & Jara-Marini, M. E. (2000) · Journal of Food Science · doi:10.1111/j.1365-2621.2000.tb15988.x · Cited by 116
Till, M. S., & Ullmann, G. M. (2009) · Journal of Molecular Modeling · doi:10.1007/s00894-009-0541-y · Cited by 115
He, S., Shi, J., Elfalleh, W., Zhang, H., Ma, Y., & Xue, S. J. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.05.156 · Cited by 108
Hu, Y., Liu, W., Yuan, C., Morioka, K., Chen, S., Liu, D., & Ye, X. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.12.006 · Cited by 106
Cui, Q., Wang, G., Gao, D. M., Wang, L., Zhang, A., Wang, X., Xu, N., & Jiang, L. (2019) · Process Biochemistry · doi:10.1016/j.procbio.2019.12.001 · Cited by 101
The effect of glycation on foam and structural properties of β-lactoglobulin
Medrano, A., Abirached, C., Panizzolo, L. A., Moyna, P., & Añón, M. C. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.07.036 · Cited by 85
Niu, H., Li, Y., Han, J., Liu, Q., & Kong, B. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.04.001 · Cited by 84
Yan, J., Li, S., Chen, G., Ma, C., McClements, D. J., Liu, X., & Liu, F. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108384 · Cited by 75
Wang, X., Du, J., Zhao, B., Wang, H., Rao, S., Du, G., Zhou, J., Chen, J., & Liu, S. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c05256 · Cited by 72
Yokoyama, K.-I., Utsumi, H., Nakamura, T., Ogaya, D., Shimba, N., Suzuki, E., & Taguchi, S. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2656-6 · Cited by 62
Wang, Z., Liang, J., Jiang, L., Li, Y., Wang, J., Zhang, H., Li, D., Han, F., Li, Q., Wang, R., et al. (2015) · CyTA - Journal of Food · doi:10.1080/19476337.2015.1011240 · Cited by 58
Effect of egg yolk on the textural, rheology and structural properties of egg gels
Zhang, M., Li, J., Chang, C., Wang, C., Li, X., Su, Y., & Yang, Y. (2018) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2018.10.024 · Cited by 58
Li, Z., Teng, F., Wang, N., Zhang, X.-N., Regenstein, J. M., Liu, J.-S., Li, Y., & Wang, Z. (2019) · Applied Sciences · doi:10.3390/app9061076 · Cited by 57
Self-citationHu, X., Hu, W.-X., Lu, H.-Y., Liu, S., Rao, S., Yang, Z., & Jiao, X. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108462 · Cited by 57
Yang, P., Wang, X., Ye, J., Rao, S., Zhou, J., Du, G., & Liu, S. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c00260 · Cited by 56
Bashash, M., Varidi, M., & Varshosaz, J. (2022) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2022.102936 · Cited by 54
Theoretical and experimental perspectives of interaction mechanism between zein and lysozyme
Huang, M. Z., Song, Y., Lv, N., Liu, C., Ren, G., Shen, Q., Wang, B., Cao, Z., & Xie, H. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107876 · Cited by 54
Murad, H. A. S., Alqurashi, T. M. A., & Hussien, M. A. (2022) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-021-03488-8 · Cited by 50
Farasat, A., Sefti, M. V., Sadeghnejad, S., & Saghafi, H. R. (2017) · Korean Journal of Chemical Engineering · doi:10.1007/s11814-017-0017-1 · Cited by 47
Zheng, N., Long, M., Zhang, Z., Osire, T., Zan, Q., Zhou, H., Du, S., & Xia, X. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108594 · Cited by 46
Self-citationZheng, N., Long, M., Zhang, Z., Zan, Q., Osire, T., Zhou, H., & Xia, X. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c06063 · Cited by 42
Self-citationWang, C., Yin, H., Zhao, Y., Zheng, Y., Xu, X., & Yue, J. (2021) · Foods · doi:10.3390/foods10030667 · Cited by 40
Wu, Z., Xie, F., Zheng, W., Liu, C., Lin, C.-P., Zheng, R., & Zheng, Y. (2023) · ACS Catalysis · doi:10.1021/acscatal.3c01469 · Cited by 40
Lefèvre, C., Bohuon, P., Lullien‐Pellerin, V., & Mestres, C. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c03553 · Cited by 39
He, M., Wu, C., Li, L., Li, Z., Tian, T., Jiang, L., Li, Y., & Teng, F. (2020) · Foods · doi:10.3390/foods10010002 · Cited by 38
Self-citationLi, S., Xie, J., Qiu, S., Xu, S., Cheng, F., Wang, Y., & Zheng, Y. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27913 · Cited by 37
Self-citationDing, X., Zeng, N., Zhang, G., Pan, J., Hu, X., & Gong, D. (2019) · Journal of Food Processing and Preservation · doi:10.1111/jfpp.14203 · Cited by 36
Liu, Y., Zhang, Y., Guo, Z., Wang, C., Kang, H., Li, J., Wang, W., Yu, L., Lu, F., & Liu, Y. (2020) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.11052 · Cited by 35
Liu, Y., Huang, L., Zheng, D., Fu, Y., Shan, M., Li, Y., Xu, Z., Jia, L., Wang, W., & Lu, F. (2018) · Food & Function · doi:10.1039/c8fo01503a · Cited by 34
Mao, Y., Zhao, C., Qi, Q., Wang, F., Xu, X., Zheng, M., Zhang, H., Wu, Y., & Liu, J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127525 · Cited by 34
Kudre, T. G., & Benjakul, S. (2013) · Food Biophysics · doi:10.1007/s11483-013-9292-5 · Cited by 31
Facile construction of fruit protein based natural hydrogel via intra/inter molecular cross-linking
Demirkıran, E., Başyi̇ğit, B., Altun, G., Yücetepe, M., Sağlam, H., & Karaaslan, M. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107899 · Cited by 31
Freeze-thaw stability of konjac glucomannan hydrogels supplemented with natural tapioca/corn starch
Li, J., Zhu, M., Gu, L., Su, Y., Yang, Y., Chang, C., & Han, Q. (2023) · LWT · doi:10.1016/j.lwt.2023.114841 · Cited by 31
The effect of transglutaminase on some quality properties of beef, chicken, and turkey meatballs
Erdem, N., Babaoğlu, A. S., Poçan, H. B., & Karakaya, M. (2020) · Journal of Food Processing and Preservation · doi:10.1111/jfpp.14815 · Cited by 31
Zhang, Z., Long, M., Zheng, N., Lü, X., Zhu, C., Osire, T., & Xia, X. (2023) · Applied and Environmental Microbiology · doi:10.1128/aem.02172-22 · Cited by 30
Self-citationFernandes, C. G., Plácido, D., Lousa, D., Brito, J. A., Isidro, A. L., Soares, C. M., Pohl, J., Carrondo, M. A., Archer, M., & Henriques, A. O. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00661 · Cited by 29
Computational approaches for understanding and predicting the self-assembled peptide hydrogels
Zhou, P., Yuan, C., & Yan, X. (2022) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2022.101645 · Cited by 29
Liu, Y., Huang, L., Shan, M., Sang, J., Li, Y., Jia, L., Wang, N., Wang, S., Shao, S., Liu, F., et al. (2019) · Biochemical Engineering Journal · doi:10.1016/j.bej.2019.107333 · Cited by 27
Xu, J., Guo, S., Li, X., Jiang, S., Zhong, X., & Zheng, Z. X. (2020) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.11025 · Cited by 27
Li, X., Fu, L., He, Z., Zeng, M., Chen, Q., Qin, F., Wang, Z., & Chen, J. (2023) · Molecules · doi:10.3390/molecules28041752 · Cited by 27
Zhang, Z., Long, M., Zheng, N., Deng, Y., Wang, Q., Osire, T., & Xia, X. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109384 · Cited by 25
Self-citationDing, C., Cai, W., Sun, J.-Y., Tao, H., & Wang, H.-L. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.109760 · Cited by 21
Liu, Z., Wang, J., Yang, C., & Wang, Z. (2023) · LWT · doi:10.1016/j.lwt.2023.115220 · Cited by 20
Han, Y., Zhu, L., Zhang, H., Liu, T., & Wu, G. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.103950 · Cited by 19
Zhang, Y., Li, C., Geary, T. G., Jardim, A., He, S., & Simpson, B. K. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107116 · Cited by 17
How fractionation procedure of mung bean protein affects transglutaminase crosslinking
Schlangen, M., Raak, N., Dinani, S. T., Corredig, M., & van der Goot, A. J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109067 · Cited by 17
Diverse models of cavity engineering in enzyme modification: Creation, filling, and reshaping
Zhang, Z., Cai, Y., Zheng, N., Deng, Y., Gao, L., Wang, Q., & Xia, X. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108346 · Cited by 17
Self-citationYadav, P., & Chowdhury, P. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12327 · Cited by 14
Gabellieri, E., Balestreri, E., Galli, A., & Cioni, P. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.128009 · Cited by 13
Zheng, N., Gao, L., Long, M., Zhang, Z., Zhu, C., Lv, X., Zhou, Q., & Xia, X. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c01684 · Cited by 12
Self-citationOta, C., Suzuki, H., Tanaka, S., & Takano, K. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b09852 · Cited by 10
Zhang, Z., Long, M., Zheng, N., Deng, Y., Wang, Q., Osire, T., & Xia, X. (2023) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12544-x · Cited by 9
Self-citationAriyoshi, R., Matsuzaki, T., Sato, R., Minamihata, K., Hayashi, K., Koga, T., Orita, K., Nishioka, R., Wakabayashi, R., Goto, M., et al. (2024) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00544 · Cited by 8
Xue, T., Zheng, X., Su, X., Chen, D., Liu, K., Yuan, X. T., Lin, R., Huang, L., He, W., Zhu, J., et al. (2020) · Food Biotechnology · doi:10.1080/08905436.2019.1711112 · Cited by 7
Statistical Analysis of the Role of Cavity Flexibility in Thermostability of Proteins
Hong, S. Y., Yoon, J., An, Y. J., Lee, S., Cha, H.-G., Pandey, A., Yoo, Y. J., & Joo, J. C. (2024) · Polymers · doi:10.3390/polym16020291 · Cited by 7
Song, X., Sheng, H., Zhou, Y., Yu, Y., He, Y., & Wang, Z. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2298 · Cited by 5
Flagged first, then by citations
Cited by
Sorted by citations
Designing 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
“Microbial TG is widely used as an enzymatic modifier to reinforce covalent crosslinking between protein molecules, thereby regulating both gel properties and digestive behavior (Deng et al. 2025 ; Y. Huang et al. 2026 ).”
Self-citationKieliszek, M. (2026) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13697-7 · Cited by 15
“Literature data (Deng et al. 2025; Mostafa 2020) confirm that mTG is widely used to restructure protein networks in various food matrices.”
Zhou, Z.-Q., Jiao, D.-Q., He, Y., Zuo, E.-H., Lu, Z., Chen, G.-G., Ding, K., & Wang, C. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c11017 · Cited by 14
Ke, C., & Pang, B. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105588 · Cited by 10
Enzymatic modification of oilseed proteins for improved functional properties
Huang, Y., Deng, Q., Chen, S., Wu, Z., Tang, X., Peng, D., Chen, Y., Wang, C., & Deng, Z. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105443 · Cited by 7
Gao, L., Wei, P., Xu, W., & Xia, X. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149052 · Cited by 7
Self-citationWang, Y., Wang, B., Zhang, G., Cheng, P., Han, J., Fu, L., & Fan, Z. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.151237 · Cited by 4
Self-citationZhu, H., Guan, K., Liu, X., Ma, Y., Lu, W., Han, X., Wang, R., & Li, Q. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148417 · Cited by 1
Preparation and Characterization of Casein–Soy Protein Hybrid Gels Cross-Linked by Transglutaminase
Ma, Y., Chen, J., Yi, M., Xiong, X., Xue, F., & Li, C. (2026) · Gels · doi:10.3390/gels12030242 · Cited by 1
“…are consistent with previous reports demonstrating that MTG can induce gelation in plant and animal proteins by catalyzing ε -( γ -glutamyl)lysine isopeptide bond formation through the γ -carboxamide groups of glutamine residues, thereby promoting intra-and intermolecular cross-linking [22].”
Chen, L., Xu, W., Gao, L., & Xia, X. (2026) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-026-00456-6 · Cited by 1
Self-citationKong, X.-X., Tang, W.-T., Li, M., Sun, Q., & Pu, C.-F. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119657 · Cited by 1
Liu, M., Chen, H., Pan, F., Yanhong, L. I. U., Yao, Y., Tian, W., Dong, B., & Zhao, G. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113068 · Cited by 1
Hu, X., Xia, C., Zhang, N., Yuan, M., Li, Z., Li, C., & Li, K. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148612 · Cited by 1
Self-citationTan, W., Zhang, Q., Wei, C., Ye, X., & Tian, J. (2026) · Journal of Food Science · doi:10.1111/1750-3841.70796
Olivo, S. D. A., & Contreras, R. A. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148701
Han, T., Chen, X., Lu, X., Qiu, T., Ye, K., Luo, L., Cheng, M., & Zhang, J. (2026) · European Food Research and Technology · doi:10.1007/s00217-026-05099-4
Li, X., Jiang, Y., & Shi, J. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149135
Zhang, Y., Jia, Y., He, X., Sun, G., Wang, K., Liu, Y., Lu, F., & Liu, Y. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112773
Luo, K., Fu, S., Xing, Y., He, X., Chen, M., Xu, Z., Jiao, Y., Cheng, Y., & Wang, X. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149363
Aggregated-state remodeling of quinoa protein gels by thermal pretreatment and transglutaminase.
Quan, Z.-Y., Ji, T., Liu, J., Zeng, D.-P., Zhang, X.-N., Chen, Y., Qian, J.-Y., & Zhang, L. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149559 · Cited by 1
Next-Generation Food Enzymology: From Metagenomic Discovery to AI-Driven Biocatalyst Design
Schwartz, M., Ladeira, R., Neiers, F., Nicolaı̈, A., Hocquet, D., & Loupiac, C. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6c04349
Hashemi, B., Assadpour, E., Tan, C., Wang, Y., & Jafari, S. M. (2026) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2026.104023
Self-citationXing, G., Sun, Y., & Liu, J. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.150829
Huang, Q., Ouyang, J., Chen, Z., Tan, M., & Cao, W. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.110034
Zhang, R., Luo, W., Sun, S., Na, X., Du, M., Zhu, B., & Wu, C. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.151666
Wang, B., Liu, Z., Su, D., Zhang, Y., & Mu, Z.-S. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113570
Metadata
- Authors
- Deng, Y., Gao, L., Zhang, Z., Guan, Z., Zheng, N., Wei, P., Du, S., Wang, Y., Li, Z., Cai, Y., & Xia, X.
- Affiliations
- Jiangnan University (CN)
- Tianjin University of Science and Technology (CN)
- Corresponding author
- Cai, Yongchao
- Xia, Xiaole
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2025-07
- Volume
- 164
- Pages
- 111170
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W4407158623
- Semantic Scholar
- f23bb6e29dd9d395b4ccaff2c388807128b96f1f
- Cited by
- 26
- References
- 72
- Citations by year
- 2026: 23 · 2025: 3
- FWCI
- 10.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Hydrocolloids (publishedVersion)
- Funders
- China Postdoctoral Science Foundation (2024M751150)
- Fundamental Research Funds for the Central Universities (JUSRP122037)
- Ministry of Science and Technology of the People's Republic of China
- National Key Research and Development Program of China (2023YFF1103703, 2021YFC2104001)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Keywords
- soy protein isolate, microbial transglutaminase, protein gelation, thermal stability, gel mechanical properties, water holding capacity, freeze-thaw stability, protein secondary structure, protein-protein interaction, gel network structure
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