Mechanisms and effects of different crosslinking degrees on gelling properties and in vitro digestibility of heat-induced microbial transglutaminase-mediated myofibrillar protein gels with or without κ-carrageenan

Hofmeister Effect‐Assisted One Step Fabrication of Ductile and Strong Gelatin Hydrogels

He, Q., Huang, Y., & Wang, S. (2017) · Advanced Functional Materials · doi:10.1002/adfm.201705069 · Cited by 511

Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties

Liu, R., Zhao, S., Xie, B., & Xiong, S. (2010) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2010.08.016 · Cited by 341

Formation and functional properties of protein–polysaccharide electrostatic hydrogels in comparison to protein or polysaccharide hydrogels

Le, X. T., Rioux, L., & Turgeon, S. L. (2016) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2016.04.006 · Cited by 333

Transglutaminase-induced gelation properties of soy protein isolate and wheat gluten mixtures with high intensity ultrasonic pretreatment

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

Steady, dynamic, and creep-recovery rheological properties of myofibrillar protein from grass carp muscle

Huang, J., Zeng, S., Xiong, S., & Huang, Q. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.04.043 · Cited by 191

Structural modification by high-pressure homogenization for improved functional properties of freeze-dried myofibrillar proteins powder

Chen, X., Zhou, R., Xu, X., Zhou, G., & Liu, D. (2017) · Food Research International · doi:10.1016/j.foodres.2017.07.007 · Cited by 176

Effects of microwave combined with conduction heating on surimi quality and morphology

Cao, H., Fan, D., Jiao, X., Huang, J., Zhao, J., Yan, B., Zhou, W., Zhang, W., & Zhang, H. (2018) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2018.01.021 · Cited by 153

Chemical interactions involved in microwave heat-induced surimi gel fortified with fish oil and its formation mechanism

Yan, B., Jiao, X., Zhu, H., Wang, Q., Huang, J., Zhao, J., Cao, H., Zhou, W., Zhang, W., Ye, W., et al. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.105779 · Cited by 153

Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation

Chin, K. B., Go, M. Y., & Xiong, Y. L. (2008) · Meat Science · doi:10.1016/j.meatsci.2008.10.012 · Cited by 142

Thermal gelling properties and structural properties of myofibrillar protein including thermo-reversible and thermo-irreversible curdlan gels

Jiang, S., Zhao, S., Jia, X., Wang, H., Zhang, H., Liu, Q., & Kong, B. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.126018 · Cited by 139

Impact of phosphates on heat-induced egg white gel properties: Texture, water state, micro-rheology and microstructure

Jin, H., Chen, J., Zhang, J., & Sheng, L. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.106200 · Cited by 130

Impact of microbial transglutaminase on 3D printing quality of Scomberomorus niphonius surimi

Dong, X., Pan, Y., Zhao, W., Huang, Y., Qu, W., Pan, J., Qi, H., & Prakash, S. (2020) · LWT · doi:10.1016/j.lwt.2020.109123 · Cited by 121

Strong fish gelatin hydrogels double crosslinked by transglutaminase and carrageenan

Chen, H., Wu, D., Ma, W., Wu, C., Liu, J., & Du, M. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.131873 · Cited by 119

The effects of three polysaccharides on the gelation properties of myofibrillar protein: Phase behaviour and moisture stability

Zhuang, X., Wang, L., Jiang, X., Chen, Y., & Zhou, G. (2020) · Meat Science · doi:10.1016/j.meatsci.2020.108228 · Cited by 113

Improvement of 3D printing performance of pea protein isolate Pickering emulsion gels by regulating electrostatic interaction between protein and polysaccharide

Wang, Y., Bai, C., Liu, W., Xu, X., Sun, Q., Jiao, B., Wang, Q., & Dai, L. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109097 · Cited by 113

Effect of different κ-carrageenan incorporation forms on the gel properties and in vitro digestibility of frankfurters

Cao, C., Yuan, D., Kong, B., Chen, Q., He, J., & Liu, Q. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107637 · Cited by 111

Transglutaminase modifies the physical stability and digestibility of chickpea protein-stabilized oil-in-water emulsions

Glušac, J., Isaschar-Ovdat, S., & Fishman, A. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126301 · Cited by 111

Innovation in the food industry using microbial transglutaminase: Keys to success and future prospects

Miwa, N. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113638 · Cited by 108

Rheological behavior of nanocellulose gels at various calcium chloride concentrations.

Qu, R., Wang, Y., Li, D., & Wang, L.-J. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118660 · Cited by 108

Textural and gel properties of frankfurters as influenced by various κ-carrageenan incorporation methods

Cao, C., Feng, Y., Kong, B., Xia, X., Liu, M., Chen, J., Zhang, F., & Liu, Q. (2021) · Meat Science · doi:10.1016/j.meatsci.2021.108483 · Cited by 106

Effects of nanofiber cellulose on functional properties of heat-induced chicken salt-soluble meat protein gel enhanced with microbial transglutaminase

Zhang, X., Wang, W., Wang, Y., Wang, Y., Wang, X., Gao, G., Chen, G., & Liu, A. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.05.046 · Cited by 100

Gel properties of myofibrillar proteins heated at different heating rates under a low-frequency magnetic field

Wang, X., Xia, M., Zhou, Y., Wang, L., Feng, X., Yang, K., Ma, J., Li, Z., Wang, L., & Sun, W. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126728 · Cited by 99

Water-soluble myofibrillar protein–pectin complex for enhanced physical stability near the isoelectric point: Fabrication, rheology and thermal property

Chen, X., Qiu, Q., Chen, K., Li, D., & Liang, L. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.10.003 · Cited by 97

Effect of microbial transglutaminase on the mechanical properties and microstructure of acid-induced gels and emulsion gels produced from thermal denatured egg white proteins

Alavi, F., Emam‐Djomeh, Z., Salami, M., & Mohammadian, M. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.008 · Cited by 96

Effects of transglutaminase coupled with κ-carrageenan on the rheological behaviours, gel properties and microstructures of meat batters

Feng, Y., Liang, X., Zhang, J., Kong, B., Shi, P., Cao, C., Zhang, H., Liu, Q., & Zhang, Y. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109265 · Cited by 95

Insight into the mechanism of myosin-fibrin gelation induced by non-disulfide covalent cross-linking

Du, J., Cao, J., Zhou, C., Pan, D., Geng, F., & Wang, Y. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111168 · Cited by 89

Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate

Wang, C., Li, T., Ma, L., Li, T., Yu, H., Hou, J., & Jiang, Z. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125757 · Cited by 88

Mechanism of low-salt surimi gelation induced by microwave heating combined with l-arginine and transglutaminase: On the basis of molecular docking between l-arginine and myosin heavy chain

Shi, T., Wang, X., Li, M., Xiong, Z., McClements, D. J., Bao, Y., Song, T., Li, J., Yuan, L., Jin, W., et al. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.133184 · Cited by 86

Raman spectroscopic study of the effects of microbial transglutaminase on heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristics

Chen, H., & Han, M. (2011) · Food Research International · doi:10.1016/j.foodres.2011.03.052 · Cited by 86

Design and characterization of low salt myofibrillar protein-sugar beet pectin double-crosslinked gels pretreated by ultrasound and konjac glucomannan: Conformational and gelling properties

Gao, Y., Wang, S., Liu, H., Gu, Y., & Zhu, J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108717 · Cited by 84

Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating

Niu, H., Li, Y., Han, J., Liu, Q., & Kong, B. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.04.001 · Cited by 84

Effects of konjac glucomannan on physical properties and microstructure of fish myofibrillar protein gel: Phase behaviours involved

Zhang, T., Chen, S., Xu, X., Zhuang, X., Chen, Y., Xue, Y., Xue, C., & Jiang, N. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108034 · Cited by 80

Elucidation of interactions between myofibrillar proteins and κ-carrageenan as mediated by NaCl level: Perspectives on multiple spectroscopy and molecular docking

Cao, C., Zhu, Z., Xue, L., Kong, B., Xu, Z., Shi, P., Li, Y., Ji, Y., Ren, Z., & Liu, Q. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125903 · Cited by 78

Insoluble dietary fibers from Lentinus edodes stipes improve the gel properties of pork myofibrillar protein: A water distribution, microstructure and intermolecular interactions study

Lu, W., Wu, D., Wang, L., Song, G., Chi, R., Ma, J., Li, Z., Wang, L., & Sun, W. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.135386 · Cited by 78

Effects of phosphorylation pretreatment and subsequent transglutaminase cross-linking on physicochemical, structural, and gel properties of wheat gluten

Zou, P., Hu, F., Ni, Z., Zhang, F., Thakur, K., Zhang, J., & Wei, Z. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.133296 · Cited by 77

Effects of microbial transglutaminase and sodium alginate on cold-set gelation of porcine myofibrillar protein with various salt levels

Hong, G. P., & Chin, K. B. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.11.011 · Cited by 75

Hofmeister effect-assisted one step fabrication of fish gelatin hydrogels

Chen, H., Shi, P., Fan, F., Chen, H., Wu, C., Xu, X., Wang, Z., & Du, M. (2019) · LWT · doi:10.1016/j.lwt.2019.108973 · Cited by 73

Synergistic recovery and enhancement of gelling properties of oxidatively damaged myofibrillar protein by -lysine and transglutaminase

Cao, Y., Li, B., Fan, X. M., Wang, J., Zhu, Z., Huang, J., & Xiong, Y. L. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129860 · Cited by 73

Mechanisms underlying the effects of ultrasound-assisted alkaline extraction on the structural properties and in vitro digestibility of Tenebrio molitor larvae protein

Zhang, F., Yue, Q., Li, X., Kong, B., Sun, F., Cao, C., Zhang, H., & Liu, Q. (2023) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2023.106335 · Cited by 71

Effects of partial substitution of NaCl on gel properties of fish myofibrillar protein during heating treatment mediated by microbial transglutaminase

Feng, J., Cao, A., Cai, L., Gong, L., Wang, J., Liu, Y., Zhang, Y., & Li, J. (2018) · LWT · doi:10.1016/j.lwt.2018.03.018 · Cited by 71

Physicochemical changes of MTGase cross-linked surimi gels subjected to liquid nitrogen spray freezing

Luo, X., Li, J., Yan, W., Liu, R., Yin, T., You, J., Du, H., Xiong, S., & Hu, Y. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.249 · Cited by 70

Changes of in vitro digestion rate and antioxidant activity of digestion products of ethanol-modified whey protein isolates

Feng, Y., Yuan, D., Cao, C., Kong, B., Sun, F., Xia, X., & Liu, Q. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107756 · Cited by 65

Expression of recombinant transglutaminase gene in Pichia pastoris and its uses in restructured meat products

Yang, X., & Zhang, Y. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.04.015 · Cited by 65

Satiety and in vitro digestibility of low saturated fat Bologna sausages added of chia mucilage powder and chia mucilage-based emulsion gel

Câmara, A. K. F. I., Geraldi, M. V., Okuro, P. K., Maróstica, M. R., Cunha, R. L., & Pollonio, M. A. R. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103753 · Cited by 64

Influence of κ-carrageenan on the rheological behaviour of a model cake flour system

Huang, M. Z., Theng, A. H. P., Yang, D., & Yang, H. (2020) · LWT · doi:10.1016/j.lwt.2020.110324 · Cited by 64

Transglutaminase-mediated crosslinking of Bambara groundnut protein hydrogels: Implications on rheological, textural and microstructural properties

Ruzengwe, F. M., Amonsou, E. O., & Kudanga, T. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109734 · Cited by 63

Impact of protein network restructured with soy protein and transglutaminase on the structural and functional characteristics of whole-grain highland barley noodle

Zhu, J., Liu, Z., Chen, L., & Zheng, B. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107909 · Cited by 61

Improved effect of flaxseed gum on the weakened gelling properties of myofibrillar protein induced by catechin

Na, J., Lin, S., Zhang, F., Zheng, D., & Liu, D. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.131136 · Cited by 60

The effect of cross‐linking degree on physicochemical properties of surimi gel as affected by MTGase

An, Y., Xiong, S., Liu, R., You, J., Yin, T., & Hu, Y. (2021) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.11274 · Cited by 57

The direct current magnetic field improved the water retention of low-salt myofibrillar protein gel under low temperature condition

Wu, D., Guo, J., Wang, X., Yang, K., Wang, L., Ma, J., Zhou, Y., & Sun, W. (2021) · LWT · doi:10.1016/j.lwt.2021.112034 · Cited by 57

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

Li, J., Zhou, Y., Li, Z., Ma, Z., Ma, Q., & Wang, L. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.136635 · Cited by 56

Interactions and phase behaviors in mixed solutions of κ-carrageenan and myofibrillar protein extracted from Alaska Pollock surimi

Zhang, T., Xu, X., Li, Z., Wang, Y., Xue, Y., & Xue, C. (2017) · Food Research International · doi:10.1016/j.foodres.2017.11.080 · Cited by 51

Thermal and physicochemical properties of red tilapia (Oreochromis niloticus) surimi gel as affected by microbial transglutaminase

Seighalani, F. Z. B., Bakar, J., Saari, N., & Khoddami, A. (2016) · Animal Production Science · doi:10.1071/an15633 · Cited by 48

Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

Sun, X. D., & Arntfield, S. D. (2011) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2011.06.019 · Cited by 48

Gel & three-dimensional printing properties of sheep plasma protein-surimi induced by transglutaminase

Yu, N., Yang, F., Gong, H., Zhou, J., Jie, C., Wang, W., Chen, X., & Sun, L. (2022) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2022.111006 · Cited by 46

Underlying mechanisms and combined effects of transglutaminase and κ-carrageenan on the quality profiles and in vitro digestibility of frankfurters

Feng, Y., Liang, X., Zhang, J., Shi, P., Cao, C., Zhang, H., Liu, Q., & Kong, B. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109344 · Cited by 46

Protein-based functional colloids and their potential applications in food: A review

Ashfaq, A., Jahan, K., Islam, R. U., & Younis, K. (2021) · LWT · doi:10.1016/j.lwt.2021.112667 · Cited by 46

Modified pea protein coupled with transglutaminase reduces phosphate usage in low salt myofibrillar gel

Dong, C., Zhao, J., Wang, L., & Jiang, J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108577 · Cited by 43

Changes of rheological behavior, thermal and microstructural properties of myofibrillar protein-κ-carrageenan mixed sol as mediated by NaCl concentration

Cao, C., Xu, Y., Kong, B., Xia, X., Chen, Q., Zhang, H., & Liu, Q. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103035 · Cited by 42

Effect of MTGase on silver carp myofibrillar protein gelation behavior after peroxidation induced by peroxyl radicals

Qian, S., Dou, P., Wang, J., Chen, L., Xu, X., Zhou, G., Zhu, B., Ullah, N., & Feng, X. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129066 · Cited by 41

In vitro trypsin digestion and identification of possible cross-linking sites induced by transglutaminase (TGase) of silver carp (Hypophthalmichthys molitrix) surimi gels with different degrees of cross-linking

Fang, M., Luo, X., Xiong, S., Yin, T., Hu, Y., Liu, R., Du, H., Liu, Y., & You, J. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130443 · Cited by 34

Dual role (promotion and inhibition) of transglutaminase in mediating myofibrillar protein gelation under malondialdehyde-induced oxidative stress

Lv, Y., Feng, X., Yang, R., Qian, S., Liu, Y., Xu, X., Zhou, G., Ullah, N., Zhu, B., & Chen, L. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129453 · Cited by 33

Effect of citrus fiber on the phosphate-mediated gel properties of myofibrillar protein and partial replacement of phosphate

Wu, Q., Zang, M., Zhao, B., Wang, S., Zhang, S., Zhu, N., Liu, M., Li, S., Lv, G., Liu, B., et al. (2022) · LWT · doi:10.1016/j.lwt.2022.114274 · Cited by 30

In-depth insight into the effects of tapioca or corn acetylated distarch phosphate on the gel properties and in vitro digestibility of kung-wan

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

In-Depth Insight into the Mechanism of Incorporation of Abelmoschus manihot Gum on the Enhancement of Gel Properties and In Vitro Digestibility of Frankfurters

Yuan, D., Liang, X., Kong, B., Sun, F., Li, X., Cao, C., & Liu, Q. (2023) · Foods · doi:10.3390/foods12071507 · Cited by 24

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

Wei, S., Xue, L., Kong, B., Cao, C., Zhang, H., Liu, Q., & Wang, H. (2023) · Meat Science · doi:10.1016/j.meatsci.2023.109265 · Cited by 23

Interplay between transglutaminase treatment and changes in digestibility of dietary proteins

Wang, Y., Xin, Q., Miao, Y., Zeng, X., Li, H., Shan, K., Nian, Y., Zhao, D., Wu, J., & Li, C. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.131446 · Cited by 22

Influence of transglutaminase treatment on the digestibility of pork longissimus dorsi proteins

Zhao, D., Wang, Y., Xin, Q., Miao, Y., Zeng, X., Shan, K., Wu, J., & Li, C. (2022) · LWT · doi:10.1016/j.lwt.2022.113378 · Cited by 13

Investigation of heat-induced pork batter quality detection and change mechanisms using Raman spectroscopy coupled with deep learning algorithms

Li, H., Wei, S., Adade, S. Y. S., Nunekpeku, X., & Chen, Q. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.140798 · Cited by 57

Effect of polysaccharide on structures and gel properties of microgel particle reconstructed soybean protein isolate/polysaccharide complex emulsion gels as solid fat mimetic

Wang, Z., Long, J., Zhang, C., Hua, Y., & Li, X. (2024) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2024.122759 · Cited by 55

Revealing the deterioration mechanism in gelling properties of pork myofibrillar protein gel induced by high-temperature treatments: Perspective on the protein aggregation and conformation

Yao, W., Zhao, Z., Zhang, J., Kong, B., Sun, F., Liu, Q., & Cao, C. (2024) · Meat Science · doi:10.1016/j.meatsci.2024.109595 · Cited by 49

Tracking protein aggregation behavior and molecular interactions induced by conformational alterations in the formation of myofibrillar protein-Abelmoschus manihot gum mixed gels during heating process

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

Effects of ultrasound-assisted emulsification and enzyme-catalyzed cross-linking on the structural, rheological and digestive properties of myofibrillar protein-peanut oleosome emulsion gels

Rahman, M., Li, R., Farooq, S., Xu, M., Fu, S., & Yu, R. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112141 · Cited by 31

Improving the Gelation Properties of Pea Protein Isolates Using Psyllium Husk Powder: Insight into the Underlying Mechanism

Chen, Q.-L., Guan, J., Wang, Z.-L., Wang, Y., Wang, X., & Chen, Z.-J. (2024) · Foods · doi:10.3390/foods13213413 · Cited by 33

Synergistic effects of κ/ι-Carrageenan and partial substitution of NaCl with MgCl2 or CaCl2 on the gel properties of myofibrillar protein

Luo, C., Wang, R., Gu, Y., Liu, X., & Zhu, J. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111279 · Cited by 24

Underlying the interactions in myofibrillar proteins and κ-carrageenan mixed sols as mediated by microbial transglutaminase based on conformational alterations, rheological behavior and molecular docking

Feng, 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

Potential mechanisms and effects of ultrasound treatment combined with pre- and post-addition of κ-carrageenan on the gelling properties and rheological behavior of myofibrillar proteins under low-salt condition.

Lin, 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

Proteomic analysis revealing mechanisms of κ-carrageenan modulating the gelling properties of heat-induced microbial transglutaminase cross-linked myofibrillar protein gels

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

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

Structuring camellia seed-derived oleosomes for the fabrication of meat analogs using transglutaminase: Structural, functional, and rheological properties

Farooq, S., Ahmad, M. I., Zheng, S., Ali, U., Zhang, Y., Xue, J., Li, Y., Shixiu, C., & Zhang, H. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111513 · Cited by 17

Incorporation of transglutaminase potentially promoted the gelling properties and sensorial attributes of lysine-rich salt-reduced frankfurters

Zhang, J., Li, X., Li, C., Kong, B., Sun, F., Cao, C., Zhang, H., Liu, Q., & Huang, X. (2025) · Food Research International · doi:10.1016/j.foodres.2025.115731 · Cited by 17

Microbial transglutaminase in food biotechnology: from biochemical mechanisms to industrial applications

Kieliszek, M. (2026) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13697-7 · Cited by 15

Abelmoschus manihot gum improves the water retention capacity of low-salt myofibrillar protein gels: Perspective on aggregation behaviour and conformational changes during heating.

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

Fabrication and characterization of double-network meat analogs based on camellia oleosomes and soy protein-wheat gluten induced by transglutaminase and calcium alginate

Farooq, S., Ahmad, M. I., Zheng, S., Ali, U., Abdullah, Xue, J., Li, Y., Shixiu, C., & Zhang, H. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143322 · Cited by 14

Underlying the regulatory mechanism of κ-carrageenan on improving the water holding capacity of myofibrillar protein gels at different NaCl levels: Emphasis on aggregation behaviour and molecular docking during heating process

Lin, 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

L-cysteine-mediated disulfide bond modulation enhances gelation behavior of ginkgo seed protein/hyaluronic acid gels.

Cheng, Q., Liu, C., Zhao, J., Zhou, F.-Z., Huang, Y., Feng, T., & Wang, Y. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.146950 · Cited by 8

Transglutaminase-enhanced walnut protein isolate gels: Synergistic effects of double modification on gelation and riboflavin encapsulation

Wang, M., Chen, R., Wu, L., Jin, F., & Wang, F. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.144247 · Cited by 8

Inclusion of chitosan in Tenebrio molitor larva protein hydrogels improved the rheological and gel properties of the composite hydrogels

Liu, M., Xu, D., Zhang, J., Pan, F., Liu, C., Li, X., Fang, X., Chen, H., Tian, W., & Peng, W. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143684 · Cited by 8

Effect and mechanism of silver carp myofibrillar protein on the properties of sturgeon myofibrillar protein during heat-induced gel formation: Protein structure and intermolecular interactions

Kong, J., Gao, P., Qixing, J., Kong, X., Ke, C., Li, S., Yang, F., Yu, P., Yu, D., Wang, H., et al. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.151126 · Cited by 5

Elucidation on molecular interaction behaviour and gelling properties of myofibrillar protein and κ-carrageenan mixed systems as modulated by microbial transglutaminase:Perspective on incubation time

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

Study on the mechanism of gel properties enhancement of Tenebrio molitor protein/chitosan composite gels induced by transglutaminase

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

The next revolution in egg product processing: Advances and future directions of egg-based fermented yogurt alternatives

Zang, J., Yan, B., Yin, Z., Tang, D., Liu, Y., Chen, J., Liu, Z., & Liu, Z. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105590 · Cited by 1

Transglutaminase dosage governs proteolytic kinetics and cleavage patterns during in vitro digestion of pea proteins: a proteomics-driven molecular analysis

Mukherjee, A., Duijsens, D., Yang, Y., Voorde, I. V. D., Fraeye, I., Weiland, F., & Grauwet, T. (2026) · International Journal of Biological Macromolecules · doi:10.2139/ssrn.6415470 · Cited by 1

Microbial transglutaminase treatment reduced the rate and extent of in vitro gastrointestinal digestion in PSE pork

Li, S., Mao, X., Zhu, J., Shan, K., Xie, Y., Zhao, D., & Li, C. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149256 · Cited by 1

Ultrasound-treated water-dispersible myofibrillar protein microgel particles: An effective strategy for stable Pickering emulsion gels with enhanced interfacial properties, dysphagia-oriented texture modification and improved encapsulation capacity

Wang, L., Li, K., Wang, Y., Ma, W., Yan, J., Han, G., Wu, H. B., & Bai, Y. (2026) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2026.107972 · Cited by 1

Influence of transglutaminase mediated crosslinking on the structure-function-digestion properties of Lupinus angustifolius protein evaluated using a multiscale approachPreprint

Mukherjee, A., Duijsens, D., Fraeye, I., Weiland, F., Grauwet, T., & Voorde, I. V. D. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.18.712645

Multiscale insights into the digestion and bioactive peptide release of Laminaria-fortified yak meat under different thermal treatments

Wang, Y., Wang, Y., Huang, X., Bai, Y., & Qi, H. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119196

Transglutaminase-induced crosslinking of soy protein isolate in crowded environments: effects of dextran concentration and molecular weight

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

Improved quality profiles and decreased in vitro digestibility of frankfurters as influenced by synergistic effects of thermo-reversible/thermo-irreversible curdlan and transglutaminase

Yuan, D., Liu, Y., Li, C., Kong, B., Cao, C., Zhang, H., Zhang, H., Liu, Q., & Feng, Y. (2026) · Meat Science · doi:10.1016/j.meatsci.2026.110165

Next-generation cellular agriculture: Innovations, challenges, and the future of animal-based food production

Nawaz, T., Latif, R., Fahad, S., Sher, M., & Zhou, R. (2026) · Cleaner Food Systems · doi:10.1016/j.clfs.2026.100056

Effects of pine needle ice structuring protein on the functional properties of myofibrillar proteins from pork patty subjected to freezing-thawing cycles

Lu, Y., Song, W., Zhao, Z., Bao, Y., Chai, Y., & Li, F. (2026) · Food Research International · doi:10.1016/j.foodres.2026.120067

Insight into synergistic effects of different charged polysaccharides toward modulating the thermal gelation characteristics of transglutaminase-mediated myofibrillar protein

Zhang, X., Wu, S., Tang, C., Yang, Z., Wang, W. C., Xu, Y., Li, C., Zhou, H. J., & Xu, B. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153713

Effects of Astragalus polysaccharides on the heat-induced gel properties and structural changes of myofibrillar proteins in low-salt concentration and its application in luncheon meat

Zhao, M., Zhang, Z., Fang, J., Huang, X., Wang, Y., Xia, X., Liu, Q., Kong, B., & Sun, F. (2026) · Meat Science · doi:10.1016/j.meatsci.2026.110218

Crosslinking-degree-dependent TGase–EGCG synergy stabilizes WPI-based walnut oil HIPPEs for use as a butter replacer

Yuan, H., Zhang, Z., Chen, K., Xiao, G., & Cheng, K. (2026) · LWT · doi:10.1016/j.lwt.2026.120125

Proteomic analysis revealing mechanisms of κ-carrageenan modulating the gelling properties of heat-induced microbial transglutaminase cross-linked myofibrillar protein gels

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

Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation

Chin, K. B., Go, M. Y., & Xiong, Y. L. (2008) · Meat Science · doi:10.1016/j.meatsci.2008.10.012 · Cited by 142

Elucidation on molecular interaction behaviour and gelling properties of myofibrillar protein and κ-carrageenan mixed systems as modulated by microbial transglutaminase:Perspective on incubation time

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

Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

Sun, X. D., & Arntfield, S. D. (2011) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2011.06.019 · Cited by 48

Research Progress on Effect of Transglutaminase-Induced Cross-Linking on Gel Properties of Myofibrillar Protein

ZHANG Jingming, F. Y. (2024) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.7506/spkx1002-6630-20230410-080