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Cited by 77Proteins in Food SystemsPolysaccharides Composition and ApplicationsFood composition and properties

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Effect of succinylation-assisted glycosylation on the structural characteristics, emulsifying, and gel properties of walnut glutenin

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Wang, Yuanli, Tao, Liang, Wang, Zilin, Wang, Yue, Lin, Xinyue, Dai, Jiahe, Shi, Chongying, Dai, Tianyi, Sheng, Jun, Tian, Yang·2024·Food Chemistry
DOI 10.1016/j.foodchem.2024.138856
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Abstract

In this study, we examined the effects of various sodium alginate (ALG) concentrations (0.2%-0.8%) on the functional and physicochemical characteristics of succinylated walnut glutenin (GLU-SA). The results showed that acylation decreased the particle size and zeta potential of walnut glutenin (GLU) by 122- and 0.27-fold, respectively. In addition, the protein structure unfolded, providing conditions for glycosylation. After GLU-SA was combined with ALG, the surface hydrophobicity decreased and the net negative charge and disulfide bond content increased. The protein structure was analyzed by FTIR, Endogenous fluorescence spectroscopy, and SEM, and ALG prompted GLU-SA cross-linking to form a stable three-dimensional network structure. The results indicated that dual modification improved the functional properties of the complex, especially its potential protein gel and emulsifying properties. This research provide theoretical support and a technical reference for expanding the application of GLU in the processing of protein and oil products.

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Research works printed but not linked: 46

  1. Basak, 2022, Succinylation of food proteins- a concise review, Lwt-Food Science and Technology, 154, 10.1016/j.lwt.2021.112866 · DOI
  2. Chakravartula, 2019, Characterization of composite edible films based on pectin/alginate/whey protein concentrate, Materials, 12, 10.3390/ma12152454 · DOI
  3. Charoensuk, 2018, Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation, International Journal of Food Properties, 21, 1633, 10.1080/10942912.2018.1502200 · DOI
  4. Chen, 2013, FTIR spectroscopic characterization of soy proteins obtained through AOT reverse micelles, Food Hydrocolloids, 31, 435, 10.1016/j.foodhyd.2012.11.017 · DOI
  5. de Souza, 2020, Effects of enzymatic extraction of oil and protein from almond cake on the physicochemical and functional properties of protein extracts, Food and Bioproducts Processing, 122, 280, 10.1016/j.fbp.2020.06.002 · DOI
  6. Dodero, 2019, A micro-rheological and rheological study of biopolymers solutions: Hyaluronic acid, Carbohydrate Polymers, 203, 349, 10.1016/j.carbpol.2018.09.072 · DOI
  7. Hadidi, 2023, Cereal bran proteins: Recent advances in extraction, properties, and applications, Critical Reviews in Food Science and Nutrition
  8. Handa, 1999, Tensile, solubility, and electrophoretic properties of egg white films as affected by surface sulfhydryl groups, Journal of Food Science, 64, 82, 10.1111/j.1365-2621.1999.tb09865.x · DOI
  9. Hattori, 1994, Functional-changes in beta-lactoglobulin by conjugation with carboxymethyl dextran, Journal of Agricultural and Food Chemistry, 42, 2120, 10.1021/jf00046a009 · DOI
  10. He, 2021, Effects of glycation and acylation on the structural characteristics and physicochemical properties of soy protein isolate, Journal of Food Science, 86, 1737, 10.1111/1750-3841.15688 · DOI
  11. Huang, 2021, Kappa-carrageenan enhances the gelation and structural changes of egg yolk via electrostatic interactions with yolk protein, Food Chemistry, 360, 10.1016/j.foodchem.2021.129972 · DOI
  12. Karimi, 2020, Characterization of disulfide (cystine) oxidation by HOCl in a model peptide: Evidence for oxygen addition, disulfide bond cleavage and adduct formation with thiols, Free Radical Biology and Medicine, 154, 62, 10.1016/j.freeradbiomed.2020.04.023 · DOI
  13. Karimi, 2016, Reactivity of disulfide bonds is markedly affected by structure and environment: Implications for protein modification and stability, Scientific Reports, 6, 10.1038/srep38572 · DOI
  14. Khanal, 2018, Modifying textural and microstructural properties of low fat Cheddar cheese using sodium alginate, Food Hydrocolloids, 83, 97, 10.1016/j.foodhyd.2018.03.015 · DOI
  15. Kim, W., Wang, Y., & Selomulya, C. (2022). Impact of sodium alginate on binary whey/pea protein-stabilised emulsions. Journal of Food Engineering, 321. https://doi.org/10.1016/j.jfoodeng.2022.110978. · DOI
  16. Kulig, 2016, Study on alginate-chitosan complex formed with different polymers ratio, Polymers, 8, 167, 10.3390/polym8050167 · DOI
  17. Lei, 2021, Physicochemical, structural and adhesion properties of walnut protein isolate-xanthan gum composite adhesives using walnut protein modified by ethanol, International Journal of Biological Macromolecules, 192, 644, 10.1016/j.ijbiomac.2021.10.022 · DOI
  18. Li, 2020, Bioactive peptides from walnut residue protein, Molecules, 25, 1285, 10.3390/molecules25061285 · DOI
  19. Li, 2022, Solubility and conformational characterization of rice glutelin after high temperature treatment, International Journal of Biological Macromolecules, 223, 1720, 10.1016/j.ijbiomac.2022.10.100 · DOI
  20. Li, 2022, Effect of glycosylation with apple pectin, citrus pectin, mango pectin and sugar beet pectin on the physicochemical, interfacial and emulsifying properties of coconut protein isolate, Food Research International, 156, 10.1016/j.foodres.2022.111363 · DOI
  21. Liu, 2022, Effects of succinylation and chitosan assembly at the interface layer on the stability and digestion characteristics of soy protein isolate-stabilized quercetin emulsions, Lwt-Food Science and Technology, 154, 10.1016/j.lwt.2021.112812 · DOI
  22. Liu, 2009, Effect of irradiation on foaming properties of egg white proteins, Poultry Science, 88, 2435, 10.3382/ps.2009-00063 · DOI
  23. Ma, 2023, Glycosylation of egg white protein with maltodextrin in the dry state: Changes in structural and gel properties, Food Chemistry, 401, 134113, 10.1016/j.foodchem.2022.134113 · DOI
  24. Meng, 2023, Effect of maillard reaction conditions on the gelation and thermal stability of whey protein isolate/D-tagatose conjugates, Food Chemistry, 405, 10.1016/j.foodchem.2022.134928 · DOI
  25. Miralles, 2007, The occurrence of a maillard-type protein-polysaccharide reaction between β-lactoglobulin and chitosan, Food Chemistry, 100, 1071, 10.1016/j.foodchem.2005.11.009 · DOI
  26. Mittal, 2023, Challenges and prospects of plant-protein-based 3D printing, Foods, 12, 10.3390/foods12244490 · DOI
  27. Montes, 2021, Impact of drying on the sodium alginate obtained after polyphenols ultrasound-assisted extraction from Ascophyllum nodosum seaweeds, Carbohydrate Polymers, 272, 10.1016/j.carbpol.2021.118455 · DOI
  28. Nahimana, 2024, Physico-chemical, functional, and structural properties of un-defatted, cold and hot defatted yellow lupin protein isolates, Food Chemistry, 437, 10.1016/j.foodchem.2023.137871 · DOI
  29. Naik, 2022, Improvements of plant protein functionalities by maillard conjugation and maillard reaction products, Critical Reviews in Food Science and Nutrition, 62, 7036, 10.1080/10408398.2021.1910139 · DOI
  30. Nawaz, 2022, Enzymatic hydrolysis improves the stability of UHT treated faba bean protein emulsions, Food and Bioproducts Processing, 132, 200, 10.1016/j.fbp.2022.01.008 · DOI
  31. Pan, 2020, Exploration of the stabilization mechanism and curcumin bioaccessibility of emulsions stabilized by whey protein hydrolysates after succinylation and glycation in different orders, Journal of Agricultural and Food Chemistry, 68, 623, 10.1021/acs.jafc.9b07350 · DOI
  32. Pu, 2019, Stability enhancement efficiency of surface decoration on curcumin-loaded liposomes: Comparison of guar gum and its cationic counterpart, Food Hydrocolloids, 87, 29, 10.1016/j.foodhyd.2018.07.039 · DOI
  33. Rygula, 2013, Raman spectroscopy of proteins: A review, Journal of Raman Spectroscopy, 44, 1061, 10.1002/jrs.4335 · DOI
  34. Sebii, 2021, Effect of succinylation on the secondary structures, surface, and thermal properties of date palm pollen protein concentrate, Journal of Food Science and Technology, 58, 632, 10.1007/s13197-020-04577-1 · DOI
  35. Shevkani, 2015, Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study, Food Hydrocolloids, 43, 679, 10.1016/j.foodhyd.2014.07.024 · DOI
  36. Sun, 2019, Effect of chemical modification on structural characteristics and functional properties of walnut glutenin, Food science, 40, 87
  37. Sze-Tao, 2000, Walnuts (Juglans regia L): Proximate composition, protein solubility, protein amino acid composition and protein in vitro digestibility, Journal of the Science of Food and Agriculture, 80, 1393, 10.1002/1097-0010(200007)80:9<1393::AID-JSFA653>3.0.CO;2-F · DOI
  38. Tirgarian, 2022, Ultra-stable high internal phase emulsions stabilized by protein-anionic polysaccharide maillard conjugates, Food Chemistry, 393, 10.1016/j.foodchem.2022.133427 · DOI
  39. Wang, 2021, Structural, gelation properties and microstructure of rice glutelin/sugar beet pectin composite gels: Effects of ionic strengths, Food Chemistry, 346, 10.1016/j.foodchem.2020.128956 · DOI
  40. Wen, 2020, Structure and functional properties of soy protein isolate-lentinan conjugates obtained in maillard reaction by slit divergent ultrasonic assisted wet heating and the stability of oil-in-water emulsions, Food Chemistry, 331, 10.1016/j.foodchem.2020.127374 · DOI
  41. Wen, 2023, Walnut protein: A rising source of high-quality protein and its updated comprehensive review, Journal of Agricultural and Food Chemistry, 71, 10525, 10.1021/acs.jafc.3c01620 · DOI
  42. Yang, S. D., Zhang, H. K., Pang X. X., Chen, Z. P., Yang, R., Zheng, W. Y., Wu, X. M., Zeng, X. A., & Liao, L (2023). Effects of Modification with Methylglyoxal on Functional Properties and Structure of Wheat Gliadin. Food Research and Development, 44(5), 48-56. https://doi.org/10.12161/j.issn.1005-6521.2023.05.008. · DOI
  43. Yu, 2022, The effect of different induction methods on the structure and physicochemical properties of glycosylated soybean isolate gels, Foods, 11, 10.3390/foods11223595 · DOI
  44. Zhang, 2023, Effects of dual succinylation and ultrasonication modification on the structural and functional properties of ovalbumin, Food Research International, 165, 10.1016/j.foodres.2023.112511 · DOI
  45. Zhang, 2012, Characterization of soy beta-conglycinin-dextran conjugate prepared by maillard reaction in crowded liquid system, Food Research International, 49, 648, 10.1016/j.foodres.2012.09.001 · DOI
  46. Zhou, 2022, Preparation and stability characterization of soybean protein isolate/sodium alginate complexes-based nanoemulsions using high-pressure homogenization, Lwt-Food Science and Technology, 154, 10.1016/j.lwt.2021.112607 · DOI

Cited by

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Metadata

Authors
Wang, Y., Tao, L., Wang, Z., Wang, Y., Lin, X., Dai, J., Shi, C., Dai, T., Sheng, J., & Tian, Y.
Affiliations
Yunnan Agricultural University (CN)
Corresponding author
  • Tao, Liang
  • Tian, Yang
ORCID
Venue
Food Chemistry
Publisher
Elsevier BV
Published
2024-07
Volume
446
Pages
138856
ISSN
0308-8146 (ISSN-L)
DOI
10.1016/j.foodchem.2024.138856
OpenAlex
W4392245183
Cited by
77
References
2
Citations by year
2026: 38 · 2025: 26 · 2024: 13
FWCI
12.99
Type
journal article
Language
en
Open access
Licence
Locations
  • Food Chemistry (publishedVersion)
  • SSRN Electronic Journal (acceptedVersion)
  • PubMed (publishedVersion)
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
succinylation, glycosylation, sodium alginate, protein cross-linking, emulsifying properties, protein gel properties, protein structure, surface hydrophobicity, zeta potential, particle size, disulfide bonds, dual modification
MeSH terms
Glutens, Glycosylation, Nuts, Juglans

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CoChat. (2026). Citation check: Effect of succinylation-assisted glycosylation on the structural characteristics, emulsifying, and gel properties of walnut glutenin. https://app.cochat.ai/papers/10.1016/j.foodchem.2024.138856
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Wang, Y., Tao, L., Wang, Z., Wang, Y., Lin, X., Dai, J., Shi, C., Dai, T., Sheng, J., & Tian, Y. (2024). Effect of succinylation-assisted glycosylation on the structural characteristics, emulsifying, and gel properties of walnut glutenin. Food Chemistry. https://doi.org/10.1016/j.foodchem.2024.138856

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