Cited by 137Proteins in Food SystemsPolysaccharides Composition and ApplicationsFood composition and properties

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Structure, gelation mechanism of plant proteins versus dairy proteins and evolving modification strategies

Tang, Qi, Roos, Yrjö H., Miao, Song·2024·Trends in Food Science & Technology

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  1. Balakrishnan, 2018, Specific effect of calcium ions on thermal gelation of aqueous micellar casein suspensions, Colloids and Surfaces B: Biointerfaces, 163, 218, 10.1016/j.colsurfb.2017.12.029 · DOI
  2. Brückner-Gühmann, 2019, Towards an increased plant protein intake: Rheological properties, sensory perception and consumer acceptability of lactic acid fermented, oat-based gels, Food Hydrocolloids, 96, 201, 10.1016/j.foodhyd.2019.05.016 · DOI
  3. Chen, 2022, Effect of moderate electric fields on the structural and gelation properties of pea protein isolate, Innovative Food Science & Emerging Technologies, 77, 10.1016/j.ifset.2022.102959 · DOI
  4. Dalgleish, 2012, The structure of the casein micelle of milk and its changes during processing, Annual Review of Food Science and Technology, 3, 449, 10.1146/annurev-food-022811-101214 · DOI
  5. Deeth, 2019, Whey proteins: An overview, Whey proteins, 1
  6. Galante, 2020, Effects of the enzymatic hydrolysis treatment on functional and antioxidant properties of quinoa protein acid-induced gels, Lwt, 118, 10.1016/j.lwt.2019.108845 · DOI
  7. Gaspar, 2015, Action of microbial transglutaminase (MTGase) in the modification of food proteins: A review, Food Chemistry, 171, 315, 10.1016/j.foodchem.2014.09.019 · DOI
  8. Ge, 2023, Understanding the differences in heat-induced gel properties of twelve legume proteins: A comparative study, Food Research International, 163, 10.1016/j.foodres.2022.112134 · DOI
  9. Gharibzahedi, 2020, The functional modification of legume proteins by ultrasonication: A review, Trends in Food Science & Technology, 98, 107, 10.1016/j.tifs.2020.02.002 · DOI
  10. Goertzen, 2021, The improvement of the functional properties of a chickpea protein isolate through proteolysis with three proteases, Cereal Chemistry, 10.1002/cche.10383 · DOI
  11. Gonzalez-Jordan, 2015, The effect of pH on the structure and phosphate mobility of casein micelles in aqueous solution, Food Hydrocolloids, 51, 88, 10.1016/j.foodhyd.2015.04.024 · DOI
  12. Hannß, 2018, Acid-induced gelation of caseins glycated with lactose: Impact of Maillard reaction-based glycoconjugation and protein cross-linking, Journal of Agricultural and Food Chemistry, 66, 11477, 10.1021/acs.jafc.8b04176 · DOI
  13. Hu, 2013, Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments, Ultrasonics Sonochemistry, 20, 187, 10.1016/j.ultsonch.2012.07.011 · DOI
  14. Hu, 2013, The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate, Food Hydrocolloids, 32, 303, 10.1016/j.foodhyd.2013.01.016 · DOI
  15. Isaschar-Ovdat, 2015, Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin, Food Hydrocolloids, 43, 493, 10.1016/j.foodhyd.2014.07.007 · DOI
  16. Jiang, 2021, Effect of acid/alkali shifting on function, gelation properties, and microstructure of Mesona chinensis polysaccharide-whey protein isolate gels, Food Hydrocolloids, 117, 10.1016/j.foodhyd.2021.106699 · DOI
  17. Juodeikiene, 2020, Functionalisation of flaxseed proteins assisted by ultrasonication to produce coatings enriched with raspberries phytochemicals, Lwt, 124, 10.1016/j.lwt.2020.109180 · DOI
  18. Kanakis, 2011, Milk β-lactoglobulin complexes with tea polyphenols, Food Chemistry, 127, 1046, 10.1016/j.foodchem.2011.01.079 · DOI
  19. Karbasi, 2019, Surface decoration of whey protein microgels through the Maillard conjugation with maltodextrin, Food Hydrocolloids, 91, 190, 10.1016/j.foodhyd.2019.01.003 · DOI
  20. Kaur, 2022, Sunflower protein isolates-composition, extraction and functional properties, Advances in Colloid and Interface Science, 306, 10.1016/j.cis.2022.102725 · DOI
  21. Kaveh, 2023, Recent advances in ultrasound application in fermented and non‐fermented dairy products: Antibacterial and bioactive properties, International Journal of Food Science and Technology, 10.1111/ijfs.16457 · DOI
  22. Kharlamova, 2019, Heat-induced gelation of mixtures of casein micelles with whey protein aggregates, Food Hydrocolloids, 92, 198, 10.1016/j.foodhyd.2019.01.048 · DOI
  23. Klost, 2019, Structure formation and rheological properties of pea protein-based gels, Food Hydrocolloids, 94, 622, 10.1016/j.foodhyd.2019.03.030 · DOI
  24. Klost, 2020, Enzymatic hydrolysis of pea protein: Interactions and protein fractions involved in fermentation induced gels and their influence on rheological properties, Food Hydrocolloids, 105, 10.1016/j.foodhyd.2020.105793 · DOI
  25. Konieczny, 2020, Nutritional properties of pea protein-enriched flour treated with different proteases to varying degrees of hydrolysis, Cereal Chemistry, 97, 429, 10.1002/cche.10258 · DOI
  26. Koutina, 2015, Influence of colloidal calcium phosphate level on the microstructure and rheological properties of rennet-induced skim milk gels, LWT-Food Science & Technology, 63, 654, 10.1016/j.lwt.2015.03.035 · DOI
  27. Lamsal, 2007, Rheological properties of soy protein hydrolysates obtained from limited enzymatic hydrolysis, LWT-Food Science & Technology, 40, 1215, 10.1016/j.lwt.2006.08.021 · DOI · Paper page
  28. Lazzaro, 2020, Tailoring the structure of casein micelles through a multifactorial approach to manipulate rennet coagulation properties, Food Hydrocolloids, 101, 10.1016/j.foodhyd.2019.105414 · DOI
  29. Le, 2017, Formation and functional properties of protein-polysaccharide electrostatic hydrogels in comparison to protein or polysaccharide hydrogels, Advances in Colloid and Interface Science, 239, 127, 10.1016/j.cis.2016.04.006 · DOI
  30. Li, 2022, Acid-induced mixed methylcellulose and casein gels: Structures, physical properties and formation mechanism, Food Chemistry, 366, 10.1016/j.foodchem.2021.130561 · DOI
  31. Li, 2023, Characterization of complex coacervation between chia seed gum and whey protein isolate: Effect of pH, protein/polysaccharide mass ratio and ionic strength, Food Hydrocolloids, 109445
  32. Li, 2022, Formation of whey protein aggregates by partial hydrolysis and reduced thermal treatment, Food Hydrocolloids, 124, 10.1016/j.foodhyd.2021.107206 · DOI
  33. Li, 2018, Effect of partial hydrolysis with papain on the characteristics of transglutaminase‐crosslinked tofu gel, Journal of Food Science, 83, 3092, 10.1111/1750-3841.14403 · DOI
  34. Li, 2019, Acid and rennet-induced coagulation behavior of casein micelles with modified structure, Food Chemistry, 291, 231, 10.1016/j.foodchem.2019.04.028 · DOI
  35. Liang, 2020, Structure, rheology and functionality of whey protein emulsion gels: Effects of double cross-linking with transglutaminase and calcium ions, Food Hydrocolloids, 102, 10.1016/j.foodhyd.2019.105569 · DOI
  36. 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
  37. Liu, 2020, Enhancing the functional characteristics of soy protein isolate via cross-linking catalyzed by Bacillus subtilis transglutaminase, Journal of the Science of Food and Agriculture
  38. Loveday, 2013, Innovative yoghurts: Novel processing technologies for improving acid milk gel texture, Trends in Food Science & Technology, 33, 5, 10.1016/j.tifs.2013.06.007 · DOI
  39. Madadlou, 2010, Acid-induced gelation behavior of sonicated casein solutions, Ultrasonics Sonochemistry, 17, 153, 10.1016/j.ultsonch.2009.06.009 · DOI
  40. Mahomud, 2017, Role of whey protein-casein complexes on yoghurt texture, Reviews in Agricultural Science, 5, 1, 10.7831/ras.5.1 · DOI
  41. Meydani, 2019, Influence of the Maillard reaction on the properties of cold-set whey protein and maltodextrin binary gels, International Dairy Journal, 90, 79, 10.1016/j.idairyj.2018.11.009 · DOI
  42. Moreira, 2019, Effect of Ohmic heating on functionality of sodium caseinate–A relationship with protein gelation, Food Research International, 116, 628, 10.1016/j.foodres.2018.08.087 · DOI
  43. Nicolai, 2019, Heat-induced gelation of plant globulins, Current Opinion in Food Science, 27, 18, 10.1016/j.cofs.2019.04.005 · DOI
  44. Nicolai, 2021, Heat-induced gelation of casein micelles, Food Hydrocolloids, 118, 10.1016/j.foodhyd.2021.106755 · DOI
  45. Nieto-Nieto, 2014, Effects of partial hydrolysis on structure and gelling properties of oat globular proteins, Food Research International, 55, 418, 10.1016/j.foodres.2013.11.038 · DOI
  46. Nieto-Nieto, 2015, Inulin at low concentrations significantly improves the gelling properties of oat protein – a molecular mechanism study, Food Hydrocolloids, 50, 116, 10.1016/j.foodhyd.2015.03.031 · DOI
  47. Nooshkam, 2020, Maillard conjugate-based delivery systems for the encapsulation, protection, and controlled release of nutraceuticals and food bioactive ingredients: A review, Food Hydrocolloids, 100, 10.1016/j.foodhyd.2019.105389 · DOI
  48. Nooshkam, 2019, The Maillard reaction products as food-born antioxidant and antibrowning agents in model and real food systems, Food Chemistry, 275, 644, 10.1016/j.foodchem.2018.09.083 · DOI
  49. Onyango, 2022, Legume protein: Properties and extraction for food applications, Vol. 2
  50. Peng, 2022, A review on the utilization of flaxseed protein as interfacial stabilizers for food applications, Journal of the American Oil Chemists' Society, 99, 723, 10.1002/aocs.12621 · DOI
  51. Permyakov, 2000, α-Lactalbumin: Structure and function, FEBS Letters, 473, 269, 10.1016/S0014-5793(00)01546-5 · DOI
  52. Qin, 2016, Transglutaminase-induced gelation properties of soy protein isolate and wheat gluten mixtures with high intensity ultrasonic pretreatment, Ultrasonics Sonochemistry, 31, 590, 10.1016/j.ultsonch.2016.02.010 · DOI
  53. Rasmussen, 1992, The multimeric structure and disulfide‐bonding pattern of bovine κ‐casein, European Journal of Biochemistry, 207, 215, 10.1111/j.1432-1033.1992.tb17040.x · DOI
  54. Ren, 2022, The influence of protease hydrolysis of lactic acid bacteria on the fermentation induced soybean protein gel: Protein molecule, peptides and amino acids, Food Research International, 111284
  55. Rodrigues, 2020, Effects of moderate electric fields on cold-set gelation of whey proteins–From molecular interactions to functional properties, Food Hydrocolloids, 101, 10.1016/j.foodhyd.2019.105505 · DOI
  56. Rodrigues, 2015, Influence of moderate electric fields on gelation of whey protein isolate, Food Hydrocolloids, 43, 329, 10.1016/j.foodhyd.2014.06.002 · DOI
  57. Salvador, 2022, Rennet-induced casein micelle aggregation models: A review, Foods, 11, 1243, 10.3390/foods11091243 · DOI
  58. Shakoor, 2022, Maillard reaction chemistry in formation of critical intermediates and flavour compounds and their antioxidant properties, Food Chemistry, 393, 10.1016/j.foodchem.2022.133416 · DOI
  59. Shanthakumar, 2022, The current situation of pea protein and its application in the food industry, Molecules, 27, 5354, 10.3390/molecules27165354 · DOI
  60. Shen, 2017, Effects of high intensity ultrasound on acid-induced gelation properties of whey protein gel, Ultrasonics Sonochemistry, 39, 810, 10.1016/j.ultsonch.2017.05.039 · DOI
  61. Shrestha, 2022, Lentil and Mungbean protein isolates: Processing, functional properties, and potential food applications, Food Hydrocolloids, 108142
  62. Spotti, 2019, Influence of Maillard reaction extent on acid induced gels of whey proteins and dextrans, Food Hydrocolloids, 91, 224, 10.1016/j.foodhyd.2019.01.020 · DOI
  63. Spotti, 2013, Gel mechanical properties of milk whey protein–dextran conjugates obtained by Maillard reaction, Food Hydrocolloids, 31, 26, 10.1016/j.foodhyd.2012.08.009 · DOI
  64. Spotti, 2017, Whey protein gelation induced by enzymatic hydrolysis and heat treatment: Comparison of creep and recovery behavior, Food Hydrocolloids, 63, 696, 10.1016/j.foodhyd.2016.10.014 · DOI
  65. Sun, 2018, Formation and structural properties of acid-induced casein–agar double networks: Role of gelation sequence, Food Hydrocolloids, 85, 291, 10.1016/j.foodhyd.2018.07.030 · DOI
  66. Surasani, 2018, Acid and alkaline solubilization (pH shift) process: A better approach for the utilization of fish processing waste and by-products, Environmental Science and Pollution Research, 25, 18345, 10.1007/s11356-018-2319-1 · DOI
  67. Tang, 2023, Effect of microbial transglutaminase on functional, rheological, and structural properties of lentil protein-casein binary gels, Food Hydrocolloids, 143, 10.1016/j.foodhyd.2023.108838 · DOI
  68. Tang, 2023, Plant protein versus dairy proteins: A pH-dependency investigation on their structure and functional properties, Foods, 12, 368, 10.3390/foods12020368 · DOI
  69. Tang, 2024, Comparative studies of structural and thermal gelation behaviours of soy, lentil and whey protein: A pH-dependency evaluation, Food Hydrocolloids, 146, 10.1016/j.foodhyd.2023.109240 · DOI
  70. Tang, 2024, Evaluation on pH-dependent thermal gelation performance of chickpea, pea protein, and casein micelles, Food Hydrocolloids, 149, 10.1016/j.foodhyd.2023.109618 · DOI
  71. Tavano, 2013, Protein hydrolysis using proteases: An important tool for food biotechnology, Journal of Molecular Catalysis B: Enzymatic, 90, 1, 10.1016/j.molcatb.2013.01.011 · DOI
  72. Thomar, 2016, Heat-induced gelation of casein micelles in aqueous suspensions at different pH, Colloids and Surfaces B: Biointerfaces, 146, 801, 10.1016/j.colsurfb.2016.07.030 · DOI
  73. Tsai, 2013, Mass spectrometry-based strategies for protein disulfide bond identification, Reviews in Analytical Chemistry, 32, 257, 10.1515/revac-2013-0011 · DOI
  74. Van de Vondel, 2021, Impact of hydrothermal treatment on denaturation and aggregation of water-extractable quinoa (Chenopodium quinoa Willd.) protein, Food Hydrocolloids, 115, 10.1016/j.foodhyd.2021.106611 · DOI
  75. Wang, 2020, Influence of Mesona blumes polysaccharide on the gel properties and microstructure of acid-induced soy protein isolate gels, Food Chemistry, 313, 10.1016/j.foodchem.2019.126125 · DOI
  76. Wang, 2022, Effects of moderate electric field on the structural properties and aggregation characteristics of soybean protein isolate, Food Hydrocolloids, 133, 10.1016/j.foodhyd.2022.107911 · DOI
  77. Wang, 2020, Effect of high intensity ultrasound on physicochemical, interfacial and gel properties of chickpea protein isolate, Lwt, 129, 10.1016/j.lwt.2020.109563 · DOI
  78. Wouters, 2016, Relevance of the functional properties of enzymatic plant protein hydrolysates in food systems, Comprehensive Reviews in Food Science and Food Safety, 15, 786, 10.1111/1541-4337.12209 · DOI
  79. Xing, 2020, Gelling behavior of bio-tofu coagulated by microbial transglutaminase combined with lactic acid bacteria, Food Research International, 134, 10.1016/j.foodres.2020.109200 · DOI
  80. Xu, 2020, Effect of enzymatic hydrolysis using endo-and exo-proteases on secondary structure, functional, and antioxidant properties of chickpea protein hydrolysates, Journal of Food Measurement and Characterization, 14, 343, 10.1007/s11694-019-00296-0 · DOI
  81. Yang, 2021, Physicochemical, rheological and digestive characteristics of soy protein isolate gel induced by lactic acid bacteria, Journal of Food Engineering, 292, 10.1016/j.jfoodeng.2020.110243 · DOI
  82. Ye, 2022, Flaxseed protein: Extraction, functionalities and applications, Food Science and Technology, 42, 10.1590/fst.22021 · DOI
  83. Yuan, 2017, Complex coacervation of soy protein with chitosan: Constructing antioxidant microcapsule for algal oil delivery, Lwt, 75, 171, 10.1016/j.lwt.2016.08.045 · DOI
  84. 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
  85. Zhang, 2022, Evaluation of dual-frequency multi-angle ultrasound on physicochemical properties of tofu gel and its finished product by TOPSIS-entropy weight method, Ultrasonics Sonochemistry, 90, 10.1016/j.ultsonch.2022.106196 · DOI
  86. Zhang, 2022, Effects of sequential enzymatic hydrolysis and transglutaminase crosslinking on functional, rheological, and structural properties of whey protein isolate, Lwt, 153, 10.1016/j.lwt.2021.112415 · DOI
  87. Zhang, 2022, Multi-dimensional analysis of rennet-induced micellar casein gels after ultrasound, International Dairy Journal, 126, 10.1016/j.idairyj.2021.105293 · DOI

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Metadata

Authors
Tang, Q., Roos, Y. H., & Miao, S.
Affiliations
  • Teagasc - The Irish Agriculture and Food Development Authority (IE)
  • University College Cork (IE)
Corresponding author
Miao, Song
Venue
Trends in Food Science & Technology
Publisher
Elsevier BV
Published
2024-05
Volume
147
Pages
104464
ISSN
0924-2244 (ISSN-L)
OpenAlex
W4393131788
Cited by
137
References
0
Citations by year
2026: 65 · 2025: 61 · 2024: 11
FWCI
29.42
Type
journal article
Language
en
Open access
closed
Locations
Trends in Food Science & Technology (publishedVersion)
Funders
TEAGASC
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
plant proteins, milk protein, protein gelation, protein structure, heat-induced gels, protein denaturation, casein micelles, protein modification, chemical modification, physical modification, biological modification, complex coacervation, enzymatic hydrolysis, transglutaminase

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