Interfacial and enhanced emulsifying behavior of phosphorylated ovalbumin

International Journal of Biological Macromolecules

Volumn 131, Issue , 2019, Pages 293-300

  Tang, Shitao ^a   Yu, Jialin ^a   Lu, Lizhi ^b   Fu, Xing ^a   Cai, Zhaoxia ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

^b INSTITUTE OF PLANT PROTECTION AND MICROBIOLOGY   (China)

Author keywords

Emulsifying properties; Ovalbumin; Wet heating phosphorylation

Indexed keywords

OVALBUMIN; PHOSPHORUS; TRIPOLYPHOSPHATE; EMULSIFYING AGENT;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROPHOBICITY; PARTICLE SIZE; PROTEIN AGGREGATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SCANNING ELECTRON MICROSCOPY; CHEMICAL PHENOMENA; CHEMISTRY; EMULSION; PHOSPHORYLATION; SPECTROSCOPY; ULTRASTRUCTURE;

EMULSIFYING AGENTS; EMULSIONS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; OVALBUMIN; PARTICLE SIZE; PHOSPHORYLATION; PROTEIN STABILITY; SPECTRUM ANALYSIS;

EID: 85062901134     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2019.03.076     Document Type: Article

References (39)

1. Hassan, N., Messina, P.V., Dodero, V.I., Ruso, J.M., Rheological properties of ovalbumin hydrogels as affected by surfactants addition. Int. J. Biol. Macromol. 48:3 (2011), 495–500.
2. Galazka, V.B., Dickinson, E., Ledward, D.A., Emulsifying properties of ovalbumin in mixtures with sulphated polysaccharides: effects of pH, ionic strength, heat and high-pressure treatment. J. Sci. Food Agric. 80:8 (2000), 1219–1229.
3. Le, F.F.C., Pezennec, S., Lechevalier, V., Beaufils, S., Desbat, B., Pézolet, M., Renault, A., Synergy between ovalbumin and lysozyme leads to non-additive interfacial and foaming properties of mixtures. Food Hydrocoll. 23:2 (2009), 352–365.
4. Matheis, G., Whitaker, J.R., Chemical phosphorylation of food proteins: an overview and a prospectus. J. Agric. Food Chem. 32:4 (1984), 699–705.
5. Joanna, C.L., Tomasz, F.C., Wojciech, R., Phosphorylation of basic amino acid residues in proteins: important but easily missed. Acta Biochim. Pol. 58:2 (2011), 137–148.
6. Huntington, J.A., Stein, P.E., Structure and properties of ovalbumin. J. Chromatogr. B Biomed. Sci. Appl. 756:1 (2001), 189–198.
7. Kinoshita-Kikuta, E., Kinoshita, E., Koike, T., Separation and identification of four distinct serine-phosphorylation states of ovalbumin by Phos-tag affinity electrophoresis. Electrophoresis 33:5 (2012), 849–855.
8. Xiong, Z., Zhang, M., Ma, M., Emulsifying properties of ovalbumin: improvement and mechanism by phosphorylation in the presence of sodium tripolyphosphate. Food Hydrocoll. 60 (2016), 29–37.
9. Xiong, Z., Ma, M., Jin, G., Xu, Q., Effects of site-specific phosphorylation on the mechanical properties of ovalbumin-based hydrogels. Int. J. Biol. Macromol. 102 (2017), 1286–1296.
10. Sheng, L., Ye, S., Han, K., Zhu, G., Ma, M., Cai, Z., Consequences of phosphorylation on the structural and foaming properties of ovalbumin under wet-heating conditions. Food Hydrocoll. 91 (2019), 166–173.
11. Zhang, K., Li, Y., Ren, Y., Research on the phosphorylation of soy protein isolate with sodium tripoly phosphate. J. Food Eng. 79:4 (2006), 1233–1237.
12. Can-Peng, L., Yoko, H., Hiroshi, S., Ibrahim, H.R., Yasushi, S., Junichi, K., Naotoshi, M., Takayoshi, A., Phosphorylation of ovalbumin by dry-heating in the presence of pyrophosphate: effect on protein structure and some properties. J. Agric. Food Chem. 53:12 (2005), 4962–4967.
13. Li, C.P., Yoko, H., Hirofumi, E., Hu, F., Yoriko, S., Masaru, T., Takayoshi, A., Phosphorylation of proteins by dry-heating in the presence of pyrophosphate and some characteristics of introduced phosphate groups. Food Chem. 114:3 (2009), 1036–1041.
14. Enomoto, H., Li, C.P., Morizane, K., Ibrahim, H.R., Sugimoto, Y., Ohki, S., Ohtomo, H., Aoki, T., Glycation and phosphorylation of beta-lactoglobulin by dry-heating: effect on protein structure and some properties. J. Agric. Food Chem., 55(6), 2007, 2392.
15. Enomoto, H., Ishimaru, T., Li, C.P., Hayashi, Y., Matsudomi, N., Aoki, T., Phosphorylation of ovalbumin by dry-heating in the presence of pyrophosphate: effect of carbohydrate chain on the phosphorylation level and heat stability. Food Chem. 122:3 (2010), 526–532.
16. Li, C.P., Chen, D., Peng, J.L., Enomoto, H., Hayashi, Y., Cong, L., Ou, L.C., Aoki, T., Improvement of functional properties of whey soy protein phosphorylated by dry-heating in the presence of pyrophosphate. LWT Food Sci. Technol. 43:6 (2010), 919–925.
17. Lei, L., Chi, Y., Improvement of functional properties of ovalbumin phosphorylated by dry-heating in the presence of pyrophosphate. Eur. Food Res. Technol. 235:5 (2012), 981–987.
18. Chen, H., Jin, Y., Ding, X., Wu, F., Bashari, M., Chen, F., Cui, Z., Xu, X., Improved the emulsion stability of phosvitin from hen egg yolk against different pH by the covalent attachment with dextran. Food Hydrocoll. 39:39 (2014), 104–112.
19. Xiong, Z., Ma, M., Enhanced ovalbumin stability at oil-water interface by phosphorylation and identification of phosphorylation site using MALDI-TOF mass spectrometry. Colloids Surf. B: Biointerfaces 153 (2017), 253–262.
20. Wang, X.B., Chi, Y.J., Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties. Czech J. Food Sci. 30:2 (2012), 99–107.
21. Hayakawa, S., Nakai, S., Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 18:4 (1985), 290–295.
22. Sheng, L., Wang, Y., Chen, J., Zou, J., Wang, Q., Ma, M., Influence of high-intensity ultrasound on foaming and structural properties of egg white. Food Res. Int., 108, 2018.
23. Li, J., Wang, X., Binding of (−)-epigallocatechin-3-gallate with thermally-induced bovine serum albumin/ι-carrageenan particles. Food Chem. 168:8 (2015), 566–571.
24. A.D. Nisbet, R.H. Saundry, A.J.G. Moir, L.A. Fothergill, J.E. Fothergill, The Complete Amino-Acid Sequence of Hen Ovalbumin.
25. Benelhadj, S., Gharsallaoui, A., Degraeve, P., Attia, H., Ghorbel, D., Effect of pH on the functional properties of Arthrospira (Spirulina) platensis protein isolate. Food Chem. 194:1 (2016), 1056–1063.
26. Li, C.P., Enomoto, H., Ohki, S., Ohtomo, H., Aoki, T., Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating. J. Dairy Sci. 88:12 (2005), 4137–4145.
27. Thaiphanit, S., Anprung, P., Physicochemical and emulsion properties of edible protein concentrate from coconut (Cocos nucifera L.) processing by-products and the influence of heat treatment. Food Hydrocoll. 52:4 (2016), 756–765.
28. Kato, A., Ibrahim, H.R., Watanabe, H., Honma, K., Kobayashi, K., New approach to improve the gelling and surface functional properties of dried egg white by heating in dry state. J. Agric. Food Chem. 37:2 (1989), 433–437.
29. Yongsawatdigul, Jirawat, Hemung, Bung-Orn, Benjakul, Soottawat, pH-dependent characteristics of gel-like emulsion stabilized by threadfin bream sarcoplasmic proteins. Food Hydrocoll. 30:1 (2013), 315–322.
30. Wan, Z.L., Wang, J.M., Wang, L.Y., Yuan, Y., Yang, X.Q., Complexation of resveratrol with soy protein and its improvement on oxidative stability of corn oil/water emulsions. Food Chem. 161:6 (2014), 324–331.
31. Khan, N.M., Mu, T.H., Zhang, M., Arogundade, L.A., The effects of pH and high hydrostatic pressure on the physicochemical properties of a sweet potato protein emulsion. Food Hydrocoll. 35:6 (2014), 209–216.
32. Wu, L., Zhao, W., Yang, R., Chen, X., Effects of pulsed electric fields processing on stability of egg white proteins. J. Food Eng. 139 (2014), 13–18.
33. Chang, C., Niu, F., Su, Y., Qiu, Y., Gu, L., Yang, Y., Characteristics and emulsifying properties of acid and acid-heat induced egg white protein. Food Hydrocoll. 54 (2016), 342–350.
34. Wang, G., Wang, T., Effects of yolk contamination, shearing, and heating on foaming properties of fresh egg white. J. Food Sci. 74:2 (2010), C147–C156.
35. Li, P., Zhuo, S., Ma, M., Jin, Y., Long, S., Effect of microwave-assisted phosphorylation modification on the structural and foaming properties of egg white powder. LWT Food Sci. Technol. 97 (2018), 151–156.
36. Huang, X., Tu, Z., Xiao, H., Wang, H., Zhang, L., Hu, Y., Zhang, Q., Niu, P., Characteristics and antioxidant activities of ovalbumin glycated with different saccharides under heat moisture treatment. Food Res. Int. 48:2 (2012), 866–872.
37. Sang-Ho, L., Thiery, L., Muriel, S., Paul, P., Changes and roles of secondary structures of whey protein for the formation of protein membrane at soy oil/water interface under high-pressure homogenization. J. Agric. Food Chem. 55:26 (2007), 10924–10931.
38. Marco-Moles, R.S., Hernando, I., Pé I., Ra, R.M., Main chemical changes in proteins and structure of egg treated with high pressure homogenisation. Czech J. Food Sci., 27(6), 2009.
39. Matsudomi, N., Nakano, K., Soma, A., Ochi, A., Improvement of gel properties of dried egg white by modification with galactomannan through the Maillard reaction. J. Agric. Food Chem. 50:14 (2002), 4113–4118.