Formation of soy protein isolate-dextran conjugates by moderate Maillard reaction in macromolecular crowding conditions

Journal of the Science of Food and Agriculture

Volumn 93, Issue 2, 2013, Pages 316-323

  Zhuo, Xiu Ying ^a   Qi, Jun Ru ^a   Yin, Shou Wei ^a   Yang, Xiao Quan ^a   Zhu, Jian Hua ^a   Huang, Li Xin ^a  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Covalent conjugate; Dextran; Macromolecular crowding; Maillard reaction; Soy protein isolate

Indexed keywords

DEXTRAN; SOYBEAN PROTEIN; VEGETABLE PROTEIN;

ARTICLE; CARBOHYDRATE DIET; CHEMISTRY; CIRCULAR DICHROISM; COMPARATIVE STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ELEMENTAL DIET; EMULSION; FOOD HANDLING; GLYCATION; GLYCOSYLATION; HEAT; ISOLATION AND PURIFICATION; MECHANICS; PH; PHYSICAL CHEMISTRY; PLIABILITY; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; TIME;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; DEXTRANS; DIETARY CARBOHYDRATES; EMULSIONS; FOOD TECHNOLOGY; FOOD, FORMULATED; GLYCOSYLATION; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; MAILLARD REACTION; MECHANICAL PHENOMENA; PHYSICOCHEMICAL PHENOMENA; PLIABILITY; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOYBEAN PROTEINS; TIME FACTORS; VEGETABLE PROTEINS;

GLYCINE MAX;

EID: 84871074672     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.5760     Document Type: Article

References (48)

1. Kato A, Sato T and Kobayashi K, Emulsifying properties of protein-polysaccharide complexes and hybrids. Agric Biol Chem 53: 2147-2152 (1989).
2. Dickinson E and Semenova MG, Emulsifying properties of covalent protein-dextran hybrids. Colloids Surf 64: 299-310 (1992).
3. Hattori M, Functional improvements in food proteins in multiple aspects by conjugation with saccharides: case studies of lactoglobulin acidic polysaccharides conjugates. Food Sci Technol Res 8: 291-299 (2002).
4. Dunlap CA and Cote GL, Lactoglobulin-dextran conjugates: effect of polysaccharide size on emulsion stability. J Agric Food Chem 53: 419-423 (2005).
5. Akhtar M and Dickinson E, Emulsifying properties of whey protein-dextran conjugates at low pH and different salt concentrations. Colloids Surf B 31: 125-132 (2003).
6. Fujiwara K, Oosawa T and Saeki H, Improved thermal stability and emulsifying properties of carp myofibrillar proteins by conjugation with dextran. J Agric Food Chem 46: 1257-1261 (1998).
7. Song Y, Babiker EE, Usui M, Saito A and Kato A, Emulsifying properties and bactericidal action of chitosan-lysozyme conjugates. Food Res Int 35: 459-466 (2002).
8. Laura JC, Mar V, Pedro J, Martin Al, Agustin O and Rosina LF, Effect of the dry-heating conditions on the glycosylation of β-lactoglobulin with dextran through the Maillard reaction. Food Hydrocolloids 19: 831-837 (2005).
9. Akhtar M and Dickinson E, Whey protein-maltodextrin conjugates as emulsifying agents: an alternative to gum Arabic. Food Hydrocolloids 21: 607-616 (2007).
10. Handa A and Kuroda N, Functional improvements in dried egg white through the Maillard-reaction. J Agric Food Chem 47: 1845-1850 (1999).
11. Kato A, Murata K and Kobayashi K, Preparation and characterization of ovalbumin-dextran conjugate having excellent emulsifying properties. J Agric Food Chem 36: 421-425 (1988).
12. Kato A, Sasaki Y, Furuta R and Kobayashi K, Functional protein-polysaccharide conjugate prepared by controlled dry-heating of ovalbumin-dextran mixture. Agric Biol Chem 54: 107-112 (1990).
13. Nakamura S, Kato A and Kobayashi K, New antimicrobial characteristics of lysozyme-dextran conjugate. J Agric Food Chem 39: 647-650 (1991).
14. Einhorn-Stoll U, Ulbrich M, Sever S and Kunzek H, Formation of milk protein-pectin conjugates with improved emulsifying properties by controlled dry heating. Food Hydrocolloids 19: 329-340 (2005).
15. Zhu D, Damodaran S and Lucey JA, Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates in aqueous solutions. J Agric Food Chem 58: 2988-2994 (2010).
16. Aoki T, Hiidome Y, Sugimoto Y, Ibrahim HR and Kato Y, Modification of ovalbumin with oligogalacturonic acids through the Maillard reaction. Food Res Int 34: 127-132 (2001).
17. Babiker EE and Kato A, Improvement of the functional properties of sorghum protein by protein-polysaccharide and protein-protein complexes. Nahrung/Food 42: 286-289 (1998).
18. Dickinson E and Galazka VB, Emulsion stabilization by ionic and covalent complexes of β-lactoglobulin with polysaccharides. Food Hydrocolloids 5: 281-296 (1991).
19. Kato A, Industrial application of Maillard-type protein-polysaccharide conjugates. Food Sci Technol Res 8: 193-199 (2002).
20. Zhu D, Damodaran S and Lucey JA, Formation of whey protein isolate (WPI)-dextran conjugates in aqueous solutions. J Agric Food Chem 56: 7113-7118 (2008).
21. Nagasawa K, Takahashi K and Hattori M, Improved emulsifying properties of β-lactoglobulin by conjugating with carboxymethyl dextran. Food Hydrocolloids 10: 63-67 (1996).
22. Minton AP, The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Agric Food Chem 276: 10577-10580 (2001).
23. Donald JW and Peter RW, Molecular crowding effects of linear polymers in protein solutions. Biophys Chem 119: 86-195 (2006).
24. Hall D and Minton AP, Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim Biophys Acta 1649: 127-139 (2003).
25. Giovanni RA and Ezio B, Thermodynamics of proteins in unusual environments. Biophys Chem 126: 65-79 (2007).
26. Diftis N and Kiosseoglou V, Physicochemical properties of dry-heated soy protein isolate-dextran mixtures. Food Chem 96: 228-233 (2006).
27. Diftis N and Kiosseoglou V, Competitive adsorption between a dry-heated soy protein-dextran mixture and surface-active materials in oil-in-water emulsions. Food Hydrocolloids 18: 639-646 (2004).
28. Diftis NG, Biliaderis CG and Kiosseoglou VD, Rheological properties and stability of model salad dressing emulsions prepared with a dry-heated soybean protein isolate-dextran mixture. Food Hydrocolloids 19: 1025-1031 (2005).
29. Qi JR, Liao JS, Yin SW, Zhu JH and Yang XQ, Formation of acid-precipitated soy protein-dextran conjugates by Maillard reaction in liquid systems. Int J Food Sci Technol 45: 2573-2580 (2010).
30. Iwabuchi S and Yamauchi F, Determination of glycinin and β-conglycinin in soybean proteins by immunmological methods. J Agric Food Chem 35: 200-205 (1987).
31. Church FC, Swaisgood H, Porter DH and Catignani GL, Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J Dairy Sci 66: 1219-1227 (1983).
32. Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970).
33. Shepherd R, Robertson A and Ofman D, Dairy glycoconjugate emulsifiers: casein-maltodextrins. Food Hydrocolloids 14: 281-286 (2000).
34. Morales FJ and Salvio FP, Free radical scavenging capacity of Maillard reaction products as related to colour and fluorescence. Food Chem 72: 119-125 (2001).
35. Kato A and Nakai S, Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim Biophys Acta 624: 13-20 (1980).
36. Hennock M, Rahalkar RR and Richmond P, Effect of xanthan gum upon the rheology and stability of oil-water emulsions. J Food Sci 49: 1271-1274 (1984).
37. Zhang GY and Foegeding EA, Heat-induced phase behavior of β-lactoglobulin polysaccharide mixtures. Food Hydrocolloids 17: 785-792 (2003).
38. Xu CH, Yu SJ and Yang XQ, The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation of β-conglycinin and glycinin. Food Res Int 43: 2270-2276 (2010).
39. Diftis N and Kiosseoglou V, Stability against heat-induced aggregation of emulsions prepared with a dry-heated soy protein isolate-dextran mixture. Food Hydrocolloids 20: 787-792 (2006).
40. Carline MJB, Bronek LW and Martinus AJS, Quantification of melanoidin concentration in sugar-casein systems. J Agric Food Chem 50: 1178-1183 (2002).
41. -) fluorescent probes. J Agric Food Chem 46: 2671-2677 (1998).
42. Cardamone M and Puri NK, Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem J 282: 589-593 (1992).
43. Oliver CM, Melton LD and Stanley RA, Functional properties of caseinate glycoconjugates prepared by controlled heating in the 'dry' state. J Sci Food Agric 86: 732-740 (2006).
44. Jing H and Kitts HH, Chemical and biochemical properties of casein-sugar Maillard reaction products. Food Cheml Toxicol 40: 1007-1015 (2000).
45. Kelly SM and Price NC, The application of circular dichroism to studies of protein folding and unfolding. Biochim Biophys Acta 1338: 161-185 (1997).
46. Zirwer D, Gast K, Welfle H, Schlesier B and Schwenke KD, Secondary structure of globulins from plant seeds: a re-evaluation from circular dichroism measurements. J Biol Macromol 7: 105-108 (1985).
47. Xu CH, Yu SJ and Yang XQ, 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 (2010).
48. Kelly SM, Jess TJ and Price NC, How to study proteins by circular dichroism. Biochim Biophys Acta 1751: 119-139 (2005).