Interface-related attributes of the Maillard reaction-born glycoproteins

Critical Reviews in Food Science and Nutrition

Volumn 58, Issue 10, 2018, Pages 1595-1603

  Karbasi, Mehri ^a   Madadlou, Ashkan ^a  

^a UNIVERSITY OF TEHRAN   (Iran)

Author keywords

conformation; hydrophobicity; interface thickness; Maltodextrin; nanoparticle; soy protein; whey protein

Indexed keywords

BIOCATALYSTS; CHEMICAL REACTIONS; CONFORMATIONS; ELECTROPHORETIC MOBILITY; EMULSIFICATION; GLYCOSYLATION; HYDROPHOBICITY; INTERFACES (MATERIALS); NANOPARTICLES; POLYSACCHARIDES;

HIGH MOLECULAR WEIGHT; HIGH PRESSURE PROCESSING; INTERFACE THICKNESS; INTERFACIAL BEHAVIORS; INTERFACIAL MEMBRANES; MALTODEXTRINS; SOY PROTEIN; WHEY PROTEINS;

PROTEINS;

GLYCOPROTEIN;

ADSORPTION; CHEMISTRY; FOOD HANDLING; GLYCATION; SURFACE PROPERTY;

ADSORPTION; FOOD TECHNOLOGY; GLYCOPROTEINS; MAILLARD REACTION; SURFACE PROPERTIES;

EID: 85020693055     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408398.2016.1270894     Document Type: Article

References (65)

1. Álvarez, C., García, V., Rendueles, M., and Díaz, M., (2012). Functional properties of isolated porcine blood proteins modified by Maillard's reaction. Food Hydrocolloid. 28(2):267–274.
2. Ames, J. M., (1992). The Maillard reaction. In: Biochemistry of Food Proteins, pp. 99–153. Hudson, B.J.F., Ed., London: Elsevier Science Publishers.
3. Amid, B. T., Mirhosseini, H., Poorazarang, H., and Mortazavi, S. A., (2013). Implications of partial conjugation of whey protein isolate to durian seed gum through maillard reactions: foaming properties, water holding capacity and interfacial activity. Molecules. 18(12):15110–15125.
4. An, Y., Cui, B., Wang, Y., Jin, W., Geng, X., Yan, X., and Li, B., (2014). Functional properties of ovalbumin glycosylated with carboxymethyl cellulose of different substitution degree. Food Hydrocolloid. 40:1–8.
5. Bu, G., Zhang, N., and Chen, F., (2015). The influence of glycosylation on the antigenicity, allergenicity, and structural properties of 11S-lactose conjugates. Food Res. Int. 76:511–517.
6. Chen, H., Jin, Y., Ding, X., Wu, F., Bashari, M., Chen, F., Cui, Z., and Xu, X., (2014). Improved the emulsion stability of phosvitin from hen egg yolk against different pH by the covalent attachment with dextran. Food Hydrocolloid. 39:104–112.
7. Chen, H., Qiu, S., Gan, J., Liu, Y., Zhu, Q., and Yin, L., (2016). New insights into the functionality of protein to the emulsifying properties of sugar beet pectin. Food Hydrocolloid. 57:262–270.
8. Chevalier, F., Chobert, J., Dalgalarrondo, M., and Haertlé, T., (2001). Characterization of the Maillard reactions products of β-lactoglobulin glucosylated in mild conditions. J. Food Biochem. 25:33–55.
9. Corzo-Martínez, M., Carrera-Sánchez, C., Villamiel, M., Rodríguez-Patino, J. M., and Moreno, F. J., (2012a). Assessment of interfacial and foaming properties of bovine sodium caseinate glycated with galactose. J. Food Eng. 113(3):461–470.
10. Corzo-Martínez, M., Sánchez, C. C., Moreno, F. J., Patino, J. M. R., and Villamiel, M., (2012b). Interfacial and foaming properties of bovine β-lactoglobulin: Galactose Maillard conjugates. Food Hydrocolloid. 27(2):438–447.
11. Dickinson, E., (2008). Interfacial structure and stability of food emulsions as affected by protein–polysaccharide interactions. Soft Matter. 4(5):932–942.
12. Dickinson, E., (2009). Hydrocolloids as emulsifiers and emulsion stabilizers. Food Hydrocolloid. 23(6):1473–1482.
13. Dickinson, E., and Semenova, M. G., (1992). Emulsifying properties of covalent protein dextran hybrids. Colloid. Surface. 64:299–310.
14. Dunlap, C. A., and Côté, G. L., (2005). β-lactoglobulin–dextran conjugates: Effect of polysaccharide size on emulsion stability. J. Agric. Food Chem. 53:419–423.
15. Fechner, A., Knoth, A., Scherze, I., and Muschiolik, G., (2007). Stability and release properties of double-emulsions stabilised by caseinate–dextran conjugates. Food Hydrocolloid. 21:943–952.
16. Gasymov, O. K., and Glasgow, B. J., (2007). ANS fluorescence: Potential to augment the identification of the external binding sites of proteins. Biochim. Biophys. Acta. 1774:403–411.
17. Gauthier, F., Bouhallab, S., and Renault, A., (2001). Modification of bovine β-lactoglobulin by glycation in a powdered state or in aqueous solution: adsorption at the air–water interface. Colloid. Surface. B. 21(1):37–45.
18. Gerrard, J. A., (2002). Protein–protein crosslinking in food: methods, consequences, applications. Trends Food Sci. Technol. 13(12):391–399.
19. Gerrard, J. A., Brown, P. K., and Fayle, S. E., (2003). Maillard crosslinking of food proteins II: the reactions of glutaraldehyde, formaldehyde and glyceraldehyde with wheat proteins in vitro and in situ. Food Chem. 80(1):35–43.
20. Gough, J. E., Scotchford, C. A., and Downes, S., (2002). Cytotoxicity of glutaraldehyde crosslinked collagen/poly (vinyl alcohol) films is by the mechanism of apoptosis. J. Biomed. Mater. Res. 61(1):121–130.
21. Guan, Y. G., Lin, H., Han, Z., Wang, J., Yu, S. J., Zeng, X. A., Liu, Y. Y., Xu, C. H., and Sun, W. W., (2010). Effects of pulsed electric field treatment on a bovine serum albumin–dextran model system, a means of promoting the Maillard reaction. Food Chem. 123(2):275–280.
22. Hiller, B., and Lorenzen, P. C., (2010). Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation. Food Res. Int. 43(4):1155–1166.
23. Kasran, M., Cui, S. W., and Goff, H. D., (2013). Emulsifying properties of soy whey protein isolate–fenugreek gum conjugates in oil-in-water emulsion model system. Food Hydrocolloid. 30(2):691–697.
24. Kester, J. J., and Richardson, T., (1984). Modification of whey proteins to improve functionality. J. Dairy Sci. 67(11):2757–2774.
25. Kim, D. Y., and Shin, W. S., (2016). Functional improvements in bovine serum albumin–fucoidan conjugate through the Maillard reaction. Food Chem. 190:974–981.
26. Kobayashi, K., Hirano, A., Ohta, A., Yoshida, T., Takahashi, K., and Hattori, M., (2001). Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. J. Agric. Food Chem. 49(2):823–831.
27. Labuza, T. P., and Baisier, W. M., (1992). The kinetics of nonenzymatic browning. In: Physical Chemistry of Foods, pp. 595–649. Schwartberg, H.G., and Hartel, R.W., Eds., New York: Marcel Dekker.
28. Li, W., Zhao, H., He, Z., Zeng, M., Qin, F., and Chen, J., (2016). Modification of soy protein hydrolysates by Maillard reaction: Effects of carbohydrate chain length on structural and interfacial properties. Colloid. Surface. B. 138:70–77.
29. Liu, J., Ru, Q., and Ding, Y., (2012). Glycation a promising method for food protein modification: physicochemical properties and structure, a review. Food Res. Int. 49(1):170–183.
30. McClements, D. J., (2004). Role of hydrocolloids as emulsifiers in foods, in Gums and Stabilizers in the Food Industry, Vol. 12. Springer Verlag, New YorkNY.
31. McClements, D. J., (2005). Food emulsions: Principles, practice and techniques (2nd ed.). CRC Press, Boca Raton, FL:.
32. Medrano, A., Abirached, C., Panizzolo, L., and Moyna, A. P. M. C., (2009). The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chem. 1131:27–133.
33. Moreno, F. J., Molina, E., Olano, A., and López-Fandiño, R., (2003). High-pressure effects on Maillard reaction between glucose and lysine. J. Agric. Food Chem. 51(2):394–400.
34. Nakai, S., and Modler, H. W., (1996). Food Proteins: Properties and Characterization. New York: John Wiley and Sons.
35. Nakamura, S., and Kato, A., (2000). Multi-functional biopolymer prepared by covalent attachment of galactomannan to egg-white proteins through naturally occurring Maillard reaction. Nahrung. 44:201–206.
36. Nakamura, S., Saito, M., Goto, T., Saeki, H., Ogawa, M., Gotoh, G., Gohya, Y., and Hwang, J. K., (2000). Rapid formation of biologically active neoglycoprotein from lysozyme and xyloglucan hydrosylates through naturally occurring Maillard reaction. Prev. Nutr. Food Sci. 5(2):65–69.
37. Nooshkam, M., and Madadlou, A., (2016a). Microwave-assisted isomerisation of lactose to lactulose and Maillard conjugation of lactulose and lactose with whey proteins and peptides. Food Chem. 200:1–9.
38. Nooshkam, M., and Madadlou, A., (2016b). Maillard conjugation of lactulose with potentially bioactive peptides. Food Chem. 192:831–836.
39. Oliveira, F. C. D., Coimbra, J. S. D. R., de Oliveira, E. B., Zuñiga, A. D. G., and Rojas, E. E. G., (2016). Food Protein-Polysaccharide Conjugates obtained via the Maillard Reaction: A Review. Crit. Rev. Food Sci. Nutr. 56(7):1108–1125.
40. Oliver, C. M., Melton, L. D., and Stanley, R. A., (2006). Creating proteins with novel functionality via the Maillard reaction: a review. Crit. Rev. Food Sci. Nutr. 46(4):337–350.
41. Patino, J. M. R., Sánchez, C. C., and Niño, M. R. R., (2008). Implications of interfacial characteristics of food foaming agents in foam formulations. Adv. Colloid Interface Sci. 140(2):95–113.
42. Pedrosa, C., De Felice, F. G., Trisciuzzi, C., and Ferreira, S. T., (2000). Selective neoglycosylation increases the structural stability of vicilin, the 7S storage globulin from pea seeds. Arch. Biochem. Biophys. 382(2):203–210.
43. Perusko, M., Al-Hanish, A., Velickovic, T. C., and Stanic-Vucinic, D., (2015). Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. Food Chem. 177:248–257.
44. Rangsansarid, J., Cheetangdee, N., Kinoshita, N., and Fukuda, K., (2008). Bovine serum albumin-sugar conjugates through the Maillard reaction: effects on interfacial behavior and emulsifying ability. J. Oleo Sci. 57(10):539–547.
45. Ruiz, G. A., Xi, B., Minor, M., Sala, G., van Boekel, M., Gogliano, V., and Stieger, M., (2016). High-pressure–high-temperature processing reduces Maillard reaction and viscosity in whey protein–sugar solutions. J. Agric. Food Chem. 64(38):7208–7215.
46. Schmitt, C., Bovay, C., and Frossard, P., (2005). Kinetics of formation and functional properties of conjugates prepared by dry-state incubation of β-lactoglobulin/acacia gum electrostatic complexes. J. Agric. Food Chem. 53(23):9089–9099.
47. Stowell, C. P., and Lee, Y. C., (1980). Neoglycoproteins: the preparation and application of synthetic glycoproteins. Adv. Carbohydr. Chem. Biochem. 37:225–281.
48. Sun-Waterhouse, D., Zhao, M., and Waterhouse, G. I., (2014). Protein modification during ingredient preparation and food processing: approaches to improve food processability and nutrition. Food Bioprocess Technol. 7(7):1853–1893.
49. Tang, C. H., Sun, X., and Foegeding, E. A., (2011). Modulation of physicochemical and conformational properties of kidney bean vicilin (phaseolin) by glycation with glucose: Implications for structure–function relationships of legume vicilins. J. Agric. Food Chem. 59(18):10114–10123.
50. Trofimova, D., and de Jongh, H. H., (2004). Modification of β-lactoglobulin by oligofructose: impact on protein adsorption at the air-water interface. Langmuir. 20(13):5544–5552.
51. Van Boekel, M. A. J. S., (2001). Kinetic aspects of the Maillard reaction: A critical review. Nahrung. 45:150–159.
52. Wong, B., (2010). Deamidated wheat protein-carbohydrate Maillard conjugates: effect of size, location and number of carbohydrate conjugated on emulsion steric stabilization at acidic pH and in ionic environment. (Doctoral dissertation, Monash University. Faculty of Science. Department of Chemistry).
53. Wong, B. T., Day, L., and Augustin, M. A., (2011). Deamidated wheat protein–dextran Maillard conjugates: effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocolloid. 25(6):1424–1432.
54. Wooster, T. J., and Augustin, M. A., (2006). β-Lactoglobulin–dextran Maillard conjugates: their effect on interfacial thickness and emulsion stability. J. Colloid Interf. Sci. 303(2):564–572.
55. Wooster, T. J., and Augustin, M. A., (2007a). Rheology of whey protein–dextran conjugate films at the air/water interface. Food Hydrocolloid. 21(7):1072–1080.
56. Wooster, T. J., and Augustin, M. A., (2007b). The emulsion flocculation stability of protein–carbohydrate diblock copolymers. J. Colloid Interf. Sci. 313(2):665–675.
57. Wu, N. N., Zhang, J. B., Tan, B., He, X. T., Yang, J., Guo, J., and Yang, X. Q., (2014a). Characterization and interfacial behavior of nanoparticles prepared from amphiphilic hydrolysates of β-conglycinin–dextran conjugates. J. Agric. Food Chem. 62(52):12678–12685.
58. Wu, S., Hu, J., Wei, L., Du, Y., Shi, X., and Zhang, L., (2014b). Antioxidant and antimicrobial activity of Maillard reaction products from xylan with chitosan/chitooligomer/glucosamine hydrochloride/taurine model systems. Food Chem. 148:196–203.
59. Xu, C. H., Yu, S. J., and Yang, X. Q., (2010). Emulsifying properties and structural characteristics of β-conglycinin and dextran conjugates synthesised in a pressurized liquid system. Int. J. Food Sci. Technol. 45:995–1001.
60. Xu, D., Wang, X., Jiang, J., Yuan, F., and Gao, Y., (2012). Impact of whey protein–Beet pectin conjugation on the physicochemical stability of β-carotene emulsions. Food Hydrocolloid. 28(2):258–266.
61. Zhang, B., Guo, X., Zhu, K., Peng, W., and Zhou, H., (2015a). Improvement of emulsifying properties of oat protein isolate–dextran conjugates by glycation. Carbohyd. Polym. 127:168–175.
62. Zhang, J. B., Wu, N. N., Yang, X. Q., He, X. T., and Wang, L. J., (2012). Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis. Food Hydrocolloid. 28(2):301–312.
63. Zhang, Y., Tan, C., Abbas, S., Eric, K., Xia, S., and Zhang, X., (2015b). Modified SPI improves the emulsion properties and oxidative stability of fish oil microcapsules. Food Hydrocolloid. 51:108–117.
64. Zhang, Y., Tan, C., Abbas, S., Eric, K., Zhang, X., Xia, S., and Jia, C., (2014). The effect of soy protein structural modification on emulsion properties and oxidative stability of fish oil microcapsules. Colloid. Surface. B. 120:63–70.
65. Zhou, H., Sun, X., Zhang, L., Zhang, P., Li, J., and Liu, Y. N., (2012). Fabrication of biopolymeric complex coacervation core micelles for efficient tea polyphenol delivery via a green process. Langmuir. 28(41):14553–14561.