Covalently cross-linked proteins & polysaccharides: Formation, characterisation and potential applications

Current Opinion in Colloid and Interface Science

Volumn 28, Issue , 2017, Pages 31-36

  Akhtar, Mahmood ^a   Ding, Rui ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Functional properties; Glycation; Maillard reaction; Protein polysaccharide conjugates

Indexed keywords

CARBOHYDRATES; CHEMICAL REACTIONS; EMULSIFICATION; FUNCTIONAL FOOD; GLYCOSYLATION; HUMIDITY CONTROL; INDUSTRIAL RESEARCH;

CONTROLLED CONDITIONS; COVALENTLY CROSS-LINKED; EMULSIFYING ACTIVITY; FUNCTIONAL PROPERTIES; GLYCATION; MAILLARD REACTION; PHYSICOCHEMICAL PROPERTY; SPINNING DISC REACTORS;

PROTEINS;

BOVINE SERUM ALBUMIN; CARBOHYDRATE; POLYSACCHARIDE; PROTEIN;

CONJUGATE; EMULSION; FOAMING; FREEZE DRYING; GEL; HUMAN; HUMIDITY; MOLECULAR WEIGHT; NONHUMAN; PH; PHYSICAL CHEMISTRY; PROTEIN CROSS LINKING; PROTEIN GLYCOSYLATION; PROTEIN INTAKE; PROTEIN STABILITY; REVIEW; SOLUBILITY; TEMPERATURE; THERMOSTABILITY; TIME;

EID: 85012065169     PISSN: 13590294     EISSN: 18790399     Source Type: Journal    
DOI: 10.1016/j.cocis.2017.01.002     Document Type: Review

References (62)

1. [1] Dickinson, E., Hydrocolloids as emulsifiers and emulsion stabilizers. Food Hydrocoll 23:6 (2009), 1473–1482.
2. [2] Dickinson, E., Hydrocolloids and emulsion stability. Phillips, G.W., Williams, Peter A., (eds.) Handbook of Hydrocolloids, 2009, Woodhead Publishing Ltd., Cambridge, 23–47.
3. [3] McClements, D., Food emulsions, vol. 24, 1999, CRC Press, Boca Raton.
4. [4••] Oliver, C.M., Melton, L.D., Stanley, R.A., Creating proteins with novel functionality via the Maillard reaction: a review. Crit Rev Food Sci Nutr 46:4 (2006), 337–350 This review shows a deeper understanding of modified properties of proteins especially from the processing condition perspectives in the Maillard reaction. Moreover, it also suggests critical factors for designing functional conjugates via the Maillard reaction.
5. [5] Liu, J., Ru, Q., Ding, Y., Glycation a promising method for food protein modification: physicochemical properties and structure, a review. Food Res Int 49:1 (2012), 170–183.
6. [6•] Dickinson, E., Interaction of polysaccharides with adsorbed proteins. Dickinson, E., (eds.) An introduction to food colloids, 1992, Oxford University Press, United States, 170 It establishes the foundation of covalently bonded protein–polysaccharide complex via the Maillard reaction by mimicking the natural material gum arabic.
7. [7] Maillard, L.C., The action of amino acids on sugar; the formation of melanoidin by a methodic route. C R Hebd Acad Sci 154 (1912), 66–68.
8. [8•] Akhtar, M., Dickinson, E., Emulsifying properties of whey protein–dextran conjugates at low pH and different salt concentrations. Colloids Surf B Biointerfaces 31:1–4 (2003), 125–132 This research paper investigates the emulsifying properties of MRPs (Maillard reaction products) under unfavourable environmental conditions, and shows that the functional properties of modified proteins can be enhanced.
9. [9•] Akhtar, M., Dickinson, E., Whey protein–maltodextrin conjugates as emulsifying agents: an alternative to gum arabic. Food Hydrocoll 21:4 (2007), 607–616 This paper is the practice of the fundamental theory (Reference No. [6]) and suggests that the conjugates have better emulsifying properties than natural gum arabic. This provides a strong evidence to support the theory and lays down a solid foundation for further research.
10. [10•] Kato, A., Murata, K., Kobayashi, K., Preparation and characterization of ovalbumin–dextran conjugate having excellent emulsifying properties. J Agric Food Chem 36:3 (1988), 421–425 This paper was published at the very beginning of the research area on modifying proteins via dry-heat treatment. It also proposed the basic structure of conjugate preparation and characterisation techniques for further researches.
11. [11••] Kato, A., Industrial applications of Maillard-type protein–polysaccharide conjugates. Food Sci Technol Res 8:3 (2002), 193–199 This review provides a summary of previous research on the topic and proposes the general mechanism of conjugate formation. Importantly, it also suggests great potential of conjugates for industrial application as a novel emulsifier and stabiliser.
12. [12] Dickinson, E., Galazka, Y.B., Emulsion stabilization by ionic and covalent complexes of beta-lactoglobulin with polysaccharides. Food Hydrocoll 5:3 (1991), 281–296.
13. [13] Du, Y., Shi, S., Jiang, Y., Xiong, H., Woo, M.W., Zhao, Q., et al. Physicochemical properties and emulsion stabilization of rice dreg glutelin conjugated with kappa-carrageenan through Maillard reaction. J Sci Food Agric 93:1 (2013), 125–133.
14. [14] Hattori, M., Aiba, Y., Nagasawa, K., Takahashi, K., Functional improvement of alginic acid by conjugating with beta-lactoglobulin. J Food Sci 61:6 (1996), 1171–1176.
15. [15] Nagasawa, K., Ohgata, K., Takahashi, K., Hattori, M., Role of the polysaccharide content and net charge on the emulsifying properties of beta-lactoglobulin-carboxymethyldextran conjugates. J Agric Food Chem 44:9 (1996), 2538–2543.
16. [16] Spotti, M.J., Perduca, M.J., Piagentini, A., Santiago, G.L., Rubiolo, A.C., Carrara, C.R., Gel mechanical properties of milk whey protein–dextran conjugates obtained by Maillard reaction. Food Hydrocoll 31:1 (2013), 26–32.
17. [17] de Oliveira, F.C., Coimbra, J.S.D., de Oliveira, E.B., Zuniga, A.D.G., Rojas, E.E.G., Food protein–polysaccharide conjugates obtained via the Maillard reaction: a review. Crit Rev Food Sci Nutr 56:7 (2016), 1108–1125.
18. [18] Kato, A., Mifuru, R., Matsudomi, N., Kobayashi, K., Functional casein–polysaccharide conjugates prepared by controlled dry heating. Biosci Biotech Bioch 56:4 (1992), 567–571.
19. [19] Jiménez-Castaño, L., Villamiel, M., López-Fandiño, R., Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass. Food Hydrocoll 21:3 (2007), 433–443.
20. [20] Kato, A., Sasaki, Y., Furuta, R., Kobayashi, K., Functional protein polysaccharide conjugate prepared by controlled dry-heating of ovalbumin dextran mixtures. Agric Biol Chem 54:1 (1990), 107–112.
21. [21] Usui, M., Tamura, H., Nakamura, K., Ogawa, T., Muroshita, M., Azakami, H., et al. Enhanced bactericidal action and masking of allergen structure of soy protein by attachment of chitosan through Maillard-type protein–polysaccharide conjugation. Nahrung 48:1 (2004), 69–72.
22. [22] Qi, J., Yang, X., Liao, J., Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction. Int J Food Sci Technol 44:11 (2009), 2296–2302.
23. [23] Li, C., Zhu, B., Xue, H., Chen, Z., Ding, Q., Wang, X., Physicochemical properties of dry-heated peanut protein isolate conjugated with dextran or gum arabic. J Am Oil Chem Soc 90:12 (2013), 1801–1807.
24. [24] Nakamura, S., Kato, A., Kobayashi, K., New antimicrobial characteristics of lysozyme dextran conjugate. J Agric Food Chem 39:4 (1991), 647–650.
25. [25] Wong, B.T., Day, L., McNaughton, D., Augustin, M.A., The effect of Maillard conjugation of deamidated wheat proteins with low molecular weight carbohydrates on the secondary structure of the protein. Food Biophys 4:1 (2009), 1–12.
26. [26] Medrano, A., Abirached, C., Panizzolo, L., Moyna, P., Anon, M.C., The effect of glycation on foam and structural properties of beta-lactoglobulin. Food Chem 113:1 (2009), 127–133.
27. [27] Gu, F.-L., Kim, J.M., Abbas, S., Zhang, X.M., Xia, S.Q., Chen, Z.X., Structure and antioxidant activity of high molecular weight Maillard reaction products from casein–glucose. Food Chem 120:2 (2010), 505–511.
28. [28•] Dickinson, E., Semenova, M.G., Emulsifying properties of covalent protein dextran hybrids. Colloids Surf 64:3–4 (1992), 299–310 This paper proposed the reasons of improved emulsifying properties of modified proteins and most importantly showed that the protein–protein interactions on the adsorbed interface were not significantly affected after the conjugation.
29. [29] Zhu, D., Damodaran, S., Lucey, J.A., Formation of whey protein isolate (WPI)–dextran conjugates in aqueous solutions. J Agric Food Chem 56:16 (2008), 7113–7118.
30. [30] Zhu, D., Damodaran, S., Lucey, J.A., Physicochemical and emulsifying properties of whey protein isolate (WPI)–dextran conjugates produced in aqueous solution. J Agric Food Chem 58:5 (2010), 2988–2994.
31. [31] Mu, L., Zhao, H., Zhao, M., Cui, C., Liu, L., Physicochemical properties of soy protein isolates–acacia gum conjugates. Czech J Food Sci 29:2 (2011), 129–136.
32. [32] Niu, L., Jiang, S., Pan, L., Zhai, Y., Characteristics and functional properties of wheat germ protein glycated with saccharides through Maillard reaction. Int J Food Sci Technol 46:10 (2011), 2197–2203.
33. [33] Burns, J.R., Jachuck, R.J.J., Recent advances on spinning disc reactor technology: better processes for bigger profits. 5th international conference on process intensification, 2003, BHR Group, Maastricht, The Netherlands.
34. [34] Jachuck, R.J., Lee, J., Kolokotsa, D., Ramshaw, C., Valachis, P., Yanniotis, S., Process intensification for energy saving. Appl Therm Eng 17 (1997), 861–867.
35. [35] Burns, J.R., Ramshaw, C., Jachuck, R.J., Measurement of liquid film thickness and the determination of spin-up radius on a rotating disc using an electrical resistance technique. Chem Eng Sci 58 (2003), 2245–2253.
36. [36] Auoune, A., Ramshaw, C., Process intensification: heat and mass transfer characteristics of liquid films on rotating discs. Int J Heat Mass Transf 42 (1999), 2543–2556.
37. [37•] Akhtar, M., Chan, P., Safriani, N., Murray, B.S., Clayton, G., Concentration of apple juice using spinning disc reactor technology. J Food Process Technol, 2(108), 2011 This research paper is not directly related to protein–polysaccharide conjugates. However, the use of the SDR (spinning disc reactor) provides a novel continuous and wet-heating process which has a great potential to optimise the preparation of protein–polysaccharide conjugates for industrial applications (see Reference No. [11]).
38. [38] Xu, C.H., Yu, S.J., Yang, X.Q., Qi, J.R., Lin, H., Zhao, Z.G., Emulsifying properties and structural characteristics of beta-conglycinin and dextran conjugates synthesised in a pressurised liquid system. Int J Food Sci Technol 45:5 (2010), 995–1001.
39. [39] Li, Z., Luo, Y., Feng, L., Effects of Maillard reaction conditions on the antigenicity of alpha-lactalbumin and beta-lactoglobulin in whey protein conjugated with maltose. Eur Food Res Technol 233:3 (2011), 387–394.
40. [40] Li, Y., Zhong, F., Ji, W., Yokoyama, W., Shoemaker, C.F., Zhu, S., et al. Functional properties of Maillard reaction products of rice protein hydrolysates with mono-, oligo- and polysaccharides. Food Hydrocoll 30:1 (2013), 53–60.
41. [41] Sun, W.-W., Yu, S.J., Yang, X.Q., Wang, J.M., Zhang, J.B., Zhang, Y., et al. Study on the rheological properties of heat-induced whey protein isolate–dextran conjugate gel. Food Res Int 44:10 (2011), 3259–3263.
42. [42] Shu, Y.W., Sahara, S., Nakamura, S., Kato, A., Effects of the length of polysaccharide chains on the functional properties of the Maillard-type lysozyme-polysaccharide conjugate. J Agric Food Chem 44:9 (1996), 2544–2548.
43. [43] Al-Hakkak, J., Al-Hakkak, F., Functional egg white–pectin conjugates prepared by controlled Maillard reaction. J Food Eng 100:1 (2010), 152–159.
44. [44] Álvarez, C., Garcia, V., Rendueles, M., Diaz, M., Functional properties of isolated porcine blood proteins modified by Maillard's reaction. Food Hydrocoll 28:2 (2012), 267–274.
45. [45] Adlernissen, J., Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27:6 (1979), 1256–1262.
46. [46] Markman, G., Livney, Y.D., Maillard-conjugate based core–shell co-assemblies for nanoencapsulation of hydrophobic nutraceuticals in clear beverages. Food Funct 3:3 (2012), 262–270.
47. [47] Church, F.C., Swaisgood, H.E., Porter, D.H., Catignani, G.L., Spectrophotometric assay using ortho-phthaldialdehyde for determination of proteolysis in milk and isolated milk-proteins. J Dairy Sci 66:6 (1983), 1219–1227.
48. [48] Nielsen, P.M., Petersen, D., Dambmann, C., Improved method for determining food protein degree of hydrolysis. J Food Sci 66:5 (2001), 642–646.
49. [49] Mengibar, M., Miralles, B., Heras, A., Use of soluble chitosans in Maillard reaction products with beta-lactoglobulin. Emulsifying and antioxidant properties. Lwt-Food Science and Technology 75 (2017), 440–446.
50. [50] Laemmli, U.K., Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature, 227(5259), 1970, 680-&.
51. [51] Kasran, M., Cui, S.W., Goff, H.D., Covalent attachment of fenugreek gum to soy whey protein isolate through natural Maillard reaction for improved emulsion stability. Food Hydrocoll 30:2 (2013), 552–558.
52. [52] Bund, T., Allelein, S., Arunkumar, A., Lucey, J.A., Etzel, M.R., Chromatographic purification and characterization of whey protein–dextran glycation products. J Chromatogr A A:1244 (2012), 98–105.
53. [53•] Corzo-Martinez, M., Carrera Sanchez, C., Javier Moreno, F., Rodriguez Patino, J.M., Villamiel, M., Interfacial and foaming properties of bovine beta-lactoglobulin: galactose Maillard conjugates. Food Hydrocoll 27:2 (2012), 438–447 This paper clearly shows the enhancement of foaming properties of modified globular proteins especially in acidic environment close to the pI of the protein.
54. [54•] Halling, P.J., Protein-stabilized foams and emulsions. CRC Crit Rev Food Sci Nutr 15:2 (1981), 155–203 This reviews presents the critical importance of protein solubility in food colloidal systems such as emulsions and foams.
55. [55] Tamnak, S., Mirhosseini, H., Tan, C.P., Ghazali, H.M., Muhammad, K., Physicochemical properties, rheological behavior and morphology of pectin–pea protein isolate mixtures and conjugates in aqueous system and oil in water emulsion. Food Hydrocoll 56 (2016), 405–416.
56. [56] Pirestani, S., Nasirpour, A., Keramat, J., Desobry, S., Effect of glycosylation with gum Arabic by Maillard reaction in a liquid system on the emulsifying properties of canola protein isolate. Carbohydr Polym 157 (2017), 1620–1627.
57. [57•] Chen, L., Chen, J.S., Wu, K.G., Yu, L., Improved low pH emulsification properties of glycated peanut protein isolate by ultrasound Maillard reaction. J Agric Food Chem 64 (2016), 5531–5538 This recent paper provides a brand new method to prepare conjugates via ultrasound Maillard reaction instead of traditional heat treatments.
58. [58] Bi, B.W., Yang, H., Fang, Y.P., Nishinari, K., Phillips, G.O., Characterization and emulsifying properties of β-lactoglobulin–gum Acacia seyal conjugates prepared via the Maillard reaction. Food Chem 214:1 (2017), 614–621.
59. [59] Lam, R.S.H., Nickerson, M.T., Food proteins: a review on their emulsifying properties using a structure–function approach. Food Chem 141:2 (2013), 975–984.
60. [60] 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.
61. [61••] Dickinson, E., Izgi, E., Foam stabilization by protein–polysaccharide complexes. Colloids Surf A Physicochem Eng Asp 113:1–2 (1996), 191–201 This paper highlights important factors for obtaining improved foaming properties of proteins: process time of preparation. Moreover, the type of protein is also critical for preparing conjugates.
62. [62••] Akinshina, A., Ettelaie, R., Dickinson, E., Smyth, G., Interactions between adsorbed layers of alpha(S1)-casein with covalently bound side chains: a self-consistent field study. Biomacromolecules 9:11 (2008), 3188–3200 This paper established a new method to investigate proteins modified with polysaccharides by computational simulation. It provided interesting evidence to explain the behaviours of conjugated proteins from theoretical point of view.