Modulation of physicochemical and conformational properties of kidney bean vicilin (phaseolin) by glycation with glucose: Implications for structure-function relationships of legume vicilins

Journal of Agricultural and Food Chemistry

Volumn 59, Issue 18, 2011, Pages 10114-10123

  Tang, Chuan He ^a   Sun, Xin ^a   Foegeding, Edward Allen ^b  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

7S globulin; conformational flexibility; emulsifying property; glycation; phaseolin; structure function relationship; vicilin

Indexed keywords

7S GLOBULIN; CONFORMATIONAL FLEXIBILITY; EMULSIFYING PROPERTY; GLYCATION; PHASEOLIN; STRUCTURE-FUNCTION RELATIONSHIP; VICILIN;

CIRCULAR DICHROISM SPECTROSCOPY; CONFORMATIONS; DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; EMULSIFICATION; GLUCOSE; OLIGOMERS; SURFACE PROPERTIES;

STRUCTURAL PROPERTIES;

EMULSIFYING AGENT; GLUCOSE; SEED STORAGE PROTEIN; VICILIN PROTEIN, PLANT;

ARTICLE; CHEMICAL PHENOMENA; CHEMISTRY; GLYCOSYLATION; PHASEOLUS; PHYSICAL CHEMISTRY; PROTEIN CONFORMATION; SOLUBILITY; SPECTROFLUOROMETRY; STRUCTURE ACTIVITY RELATION;

EMULSIFYING AGENTS; GLUCOSE; GLYCOSYLATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; PHASEOLUS; PHYSICOCHEMICAL PHENOMENA; PROTEIN CONFORMATION; SEED STORAGE PROTEINS; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP;

PHASEOLUS VULGARIS;

EID: 80053107915     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf202517f     Document Type: Article

References (40)

1. Maruyama, N.; Katsube, T.; Wada, Y.; Oh, M. H.; Barba de la Rosa, A. P.; Okuda, E.; Nakagawa, S.; Utsumi, S. The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features Eur. J. Biochem. 1998, 258, 854-862 (Pubitemid 28557955)
2. Maruyama, N.; Salleh, M. R. M.; Takahashi, K.; Yagasaki, K.; Goto, H.; Hontani, N.; Nakagawa, S.; Utsumi, S. Structure-physicochemical function relationships of soybean β-conglycinin heterotrimers J. Agric. Food Chem. 2000, 50, 4323-4326 (Pubitemid 34756034)
3. Maruyama, N.; Sato, R.; Wada, Y.; Matsumura, Y.; Goto, H.; Okuda, E.; Nakagawa, S.; Utsumi, S. Structure-physicochemical function relationships of soybean β-conglycinin constituent subunits J. Agric. Food Chem. 1999, 47, 5278-5284 (Pubitemid 30016975)
4. Maruyama, N.; Salleh, M. R. M.; Takahashi, K.; Yagasaki, K.; Goto, H.; Hontani, N.; Nakagawa, S.; Utsumi, S. The effect of N-linked glycans on structural features and physicochemical functions of soybean β-conglycinin homotrimers J. Am. Oil Chem. Soc. 2002, 79, 39-144
5. Garcia, R. N.; Adachi, M.; Tecson-Mendoza, E. M.; Bernardo, A. E. N.; Utsumi, S. Physicochemical properties of native and recombinant mungbean (Vigna radiate L. Wilczek) 8S globulins and the effects of the N-linked glycans J. Agric. Food Chem. 2006, 54, 6005-6010 (Pubitemid 44342234)
6. Yin, S. W.; Tang, C. H.; Wen, Q. B.; Yang, X. Q. Functional and conformational properties of phaseolin (Phaseolus vulgris L.) and kidney bean protein isolate: a comparative study J. Sci. Food Agric. 2010, 90, 599-607
7. Tang, C. H.; Sun, X. Physicochemical and structural properties of 8S and/or 11S globulins from mungbean [ Vigna radiate (L.) Wilczek] with various polypeptide constituents J. Agric. Food Chem. 2010, 58, 6395-6402
8. Tang, C. H.; Sun, X. Structure-physicochemical function relationships of 7S globulins (vicilins) from red bean (Phaseolus angularis) with different polypeptide constituents Food Hydrocolloids 2011, 25, 536-544
9. Tang, C. H.; Sun, X. A comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes: implications for the structure-function relationship Food Hydrocolloids 2011, 25, 315-324
10. Kimura, A.; Fukuda, T.; Zhang, M.; Motoyama, S.; Maruyama, N.; Utsumi, S. Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean - French bean 7S globulin exhibits excellent properties J. Agric. Food Chem. 2008, 56, 10273-10279
11. Jivotovskaya, A. V.; Vitalyi, I. S.; Vitalyi, I. R.; Horstmann, C.; Vaintraub, I. A. Proteolysis of phaseolin in relation to its structure J. Agric. Food Chem. 1996, 44, 3768-3772 (Pubitemid 126453365)
12. 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. 2006, 46, 337-350
13. Caer, D.; Baniel, A.; Subirade, M.; Guéguen, J.; Colas, B. Preparation and physicochemical properties of glycated derivatives of pea legumin J. Agric. Food Chem. 1990, 38, 1700-1706
14. Baniel, A.; Caer, D.; Colas, B.; Guéguen, J. Functional properties of glycated derivatives of the 11S storage protein from pea (Pisum sativum L.) J. Agric. Food Chem. 1992, 40, 200-205
15. Pedrosa, C.; Trisciuzzi, C.; Ferreira, S. Effects of glycosylation on functional properties of vicilin, the 7S storage globulin from pea (Pisum sativum) J. Agric. Food Chem. 1997, 45, 2025-2030 (Pubitemid 127485518)
16. Pedrosa, C.; De Felice, F.; Trisciuzzi, C.; Ferreira, S. Selective neoglycation increases the structural stability of vicilin, the 7S storage globulin from pea seeds Arch. Biochem. Biophys. 2000, 382, 203-210
17. Achouri, A.; Boye, J. I.; Yaylayan, V. A.; Yeboah, F. Functional properties of glycated soy 11S glycinin J. Food Sci. 2005, 70, C269-C274
18. Hall, T. C.; McLeester, R. C.; Bliss, F. A. Equal expression of the maternal and paternal alleles for the polypeptide subunits of the major storage protein of the bean Phaseolus vulgaris L Plant Physiol. 1977, 59, 1122-1124
19. Habeeb, A. F. S. A. Determination of free amino groups in proteins by trinitrobenzensulfonic acid Anal. Biochem. 1966, 14, 328-336
20. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227, 681-685
21. -) fluorescent probes J. Agric. Food Chem. 1998, 46, 2671-2677 (Pubitemid 128488354)
22. Lowry, O. H.; Rosebrough, H. J.; Lewis, A.; Randall, R. J. Protein measurement with the Folin phenol reagent J. Biol. Chem. 1951, 19, 265-275
23. Pearce, K. N.; Kinsella, J. E. Emulsifying properties of proteins: evaluation of a turbidimetric technique J. Agric. Food Chem. 1978, 26, 716-723
24. Cameron, D. R.; Weber, M. E.; Idziak, E. S.; Neufeld, R. J.; Cooper, D. G. Determination of interfacial areas in emulsions using turbidimetric and droplet size data:cCorrection of the formula for emulsifying activity index J. Agric. Food Chem. 1991, 39, 655-659
25. Sreerama, N.; Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set Anal. Biochem. 2000, 287, 252-260 (Pubitemid 32006234)
26. van de Lagemaat, J.; Silván, J. M.; Moreno, F. J.; Olano, A.; de Castillo, M. D. In vitro glycation and antigenicity of soy proteins Food Res. Int. 2007, 40, 153-160 (Pubitemid 44738542)
27. Carbonaro, M. 7S globulins from Phaseolus vulgaris L.: impact of structural aspects on the nutritional quality Biosci., Biotechnol., Biochem. 2006, 70, 2620-2626 (Pubitemid 44819830)
28. Li, Y.; Lu, F.; Luo, C.; Chen, Z.; Mao, J.; Shoemaker, C.; Zhong, F. Functional properties of the Maillard reaction products of rice protein with sugar Food Chem. 2009, 117, 69-74
29. Schwenke, K. D. Reflections about the functional potential of legume proteins. A review Nahrung/Food 2001, 45, 377-381 (Pubitemid 33625121)
30. Kelly, S. M.; Price, N. C. The application of circular dichroism to studies of protein folding and unfolding Biochim. Biophys. Acta 1997, 1338, 161-185 (Pubitemid 27156998)
31. Zirwer, D.; Gast, K.; Welfle, H.; Schlesier, B.; Schwenke, K. D. Secondary structure of globulins from plant seeds: a re-evaluation from circular dichroism measurements Int. J. Biol. Macromol. 1985, 7, 105-108
32. Yang, J. T.; Wu, C.-S.; Martinez, H. M. Calculation of protein conformation from circular dichroism Methods Enzymol. 1986, 130, 208-269
33. DiLollo, A.; Alli, I.; Biliarderis, C.; Barakur, N. Thermal and surface active properties of citric acid-extracted and alkali-extracted proteins from Phaseolus beans J. Agric. Food Chem. 1993, 41, 24-29
34. Arntfield, S. D.; Murray, E. D. The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indictor of protein denaturation Can. Int. Food Sci. Technol. J. 1981, 14, 289-294
35. Privalov, P. L. Stability of proteins: proteins which do not present a single cooperative system Adv. Protein Chem. 1982, 35, 1-104
36. Pallarès, I.; Vendrell, J.; Avilès, F. X.; Ventura, S. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin J. Mol. Biol. 2004, 342, 321-331 (Pubitemid 39094523)
37. Dufour, E.; Hoa, G. H.; Haertlé, T. High-pressure effects of β-lactoglobulin interactions with ligands studied by fluorescence Biochim. Biophys. Acta 1994, 1206, 166-172
38. Yin, S. W.; Tang, C. H.; Wen, Q. B.; Yang, X. Q.; Yuan, D. B. The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates Food Res. Int. 2010, 43, 730-738
39. Kelly, S. M.; Jess, T. J.; Price, N. C. How to study proteins by circular dichroism? Biochim. Biophys. Acta 2005, 1751, 119-139 (Pubitemid 41112231)
40. Moure, A.; Sineiro, J.; Dominguez, H.; Parajo, J. C. Functionality of oilseed protein products: a review Food Res. Int. 2006, 39, 945-963 (Pubitemid 44397553)