Functional and conformational properties of phaseolin (Phaseolus vulgris L.) and kidney bean protein isolate: A comparative study

Journal of the Science of Food and Agriculture

Volumn 90, Issue 4, 2010, Pages 599-607

  Yin, Shou Wei ^a   Tang, Chuan He ^a   Wen, Qi Biao ^a   Yang, Xiao Quan ^a  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Acid extraction technique; Conformation; Functional property; Phaseolin; Protein isolate; Red kidney bean (Phaseolus vulgaris L.)

Indexed keywords

DISULFIDE; DITHIOTHREITOL; PLANT EXTRACT; THIOL DERIVATIVE; VEGETABLE PROTEIN; EMULSION; GEL;

ARTICLE; BEAN; CHEMISTRY; CIRCULAR DICHROISM; COMPARATIVE STUDY; DIFFERENTIAL SCANNING CALORIMETRY; EMULSION; GEL; ISOLATION AND PURIFICATION; PLANT SEED; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; SPECTROFLUOROMETRY; PHASEOLUS;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; DISULFIDES; DITHIOTHREITOL; EMULSIONS; GELS; PHASEOLUS; PLANT EXTRACTS; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SEEDS; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL COMPOUNDS;

PHASEOLUS VULGARIS;

EID: 76749106479     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3856     Document Type: Article

References (39)

1. FAO. Food and Agricultural Organization of the United Nations. [online] Agriculture bulletin Board on Data Collection, Dissemination and Quality of Statistics (2002). Available: URL: http//apps.fao.org/cgibin/nph-db.pI?subset=agriculture [1August 2002].
2. Sathe SK, Dry bean protein functionality. Crit Rev Biotechnol 22:175-223 (2002).
3. Tang CH, Thermal denaturation and gelation of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study. LWTFood Sci Technol 41:1380-1388 (2008).
4. Rangel A, Domont GB, Pedrosa C and Ferreira ST, Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate. J Agric Food Chem 51:5792-5797 (2003).
5. Tang CH, Sun X, Yin SW and Ma CY, Transglutaminase-induced crosslinking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibility. Food Res Int 41:941-947 (2008).
6. Yin SW, Tang CH, Wen QB, Yang XQ and Li L, Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: Effect of high-pressure treatment. Food Chem 110:938-945 (2008).
7. Bollini R and Vitale A, Genetic variability in charge micro heterogeneity and polypeptide compositions of Phaseolus vulgaris; and peptide maps of its three major subunits. Plant Physiol 52:96-1003 (1981).
8. Hall TC, McLeester RC and Bliss FA, 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 59:1122-1124 (1977).
9. Romero J, Sun SM, McLeester RC, Bliss FA and Hall TC, Heritable variation in a polypeptide subunit of the major storage protein of the bean, Phaseolus vulgaris L. Plant Physiol 56:776-779 (1975).
10. Sun SM, McLeester RC, Bliss FA and Hall TC, Reversible and irreversible dissociation of globulins from Phaseolus vulgaris seed. J Biol Chem 249:2118-2121 (1974).
11. McLeester RC, Hall TC, Sun SM and Bliss FA, Comparison of globulin proteins from Phaseolus vulgaris with those from Vicia faba. Phytochemistry 12:85-93 (1973).
12. Sun SM, McLeester RC, Bliss FA and Hall TC, Heritable variation in a polypeptide subunit of the major storage protein of the bean (Phaseolus vulgaris L.). Plant Physiol 56:776-779 (1974).
13. Sun SM and Hall TC, Solubility characteristics of globulins from Phaseolus seeds in regard to their isolation and characterization. J Agric Food Chem 23:184-189 (1975).
14. Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685 (1970).
15. Lowry OH, Rosembroug HJ, Lewis A and Randall RJ, Protein measurement with the Folin Phenol reagent. J Biol Chem 19:265-275 (1951).
16. Pearce KN and Kinsella JE, Emulsifying properties of proteins: Evaluation of a turbidimetric technique. J Agric Food Chem 26:716-723 (1978).
17. Ellman GD, Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-72 (1959).
18. Beveridge T, Toma SJ and Nakai S, Determination of SH and S enbond S groups in some food proteins using Ellman's reagent. J Food Sci 39:49-51 (1974).
19. Thannhauser TW, Konishi Y and Scheraga HA, Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins. Anal Chem 138:181-188 (1984).
20. Petruccelli S and Añón MC, Partial reduction of soy protein isolate disulfide bonds. J Agric Food Chem 43:2001-2006 (1995).
21. Kato A and Nakai S, Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. BiochimBiophys Acta 624:13-20 (1980).
22. Haskard CA and Li-Chan ECY, Hydophobicity of bovine serumalbumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes. JAgricFoodChem 46:2671-2677 (1998).
23. Montoya CA, Lalle's JP, Beebe S, Montagne L, Souffrant WB, and Leterme P, Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats. Br J Nutr 95:116-123 (2006).
24. Montoya CA, Lalle's JP, Beebe S, Montagne L, Souffrant WB, and Leterme ??, In vitroandin vivo proteinhydrolysisofbeans (Phaseolus vulgaris L) genetically modified to express different phaseolin types. Food Chem 106:1225-1233 (2008).
25. Shi J, Xue SJ, Kakuda Y, Ilic S and Kim D, Isolation and characterization of lectins from kidney beans (Phaseolus vulgaris). Process Biochem (Oxford UK) 42:1436-1442 (2007).
26. Genovese MI and Lajol FM, Influence of naturally acid-soluble proteins from beans (Phaseolus vulgaris L.) on in vitro digestibility determination. Food Chem 62:315-323 (1998).
27. Arntfield SD and Murray ED, The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Can Inst Food Sci Technol J 14:289-294 (1981).
28. Kinsella JE, Relationship between structure and functional properties of food proteins, in Food Proteins, ed. by Fox PF and Cowden JJ. Applied Science Publishers, London, pp. 51-103 (1982).
29. Cheftal JC, Cuq JL and Lorient D, Amino acids, peptides, and proteins, in Food Chemistry, ed. by Fennema OR. Marcel Dekker, New York, pp. 246-369 (1985).
30. Steinhardt J. The nature of specific and non-specific interactions of detergent with protein: complexing and unfolding, in Protein-Ligand Interaction, ed. by Sund H and Blauer G. de Gruyter, Berlin, pp. 412-426 (1975).
31. Li-Chan ECY and Ma CY, Thermal analysis of flaxseed (Linum usitatissimum) proteins by differential scanning calorimetry. Food Chem 77:495-502 (2002).
32. Meng GT and Ma CY, Thermal properties of Phaseolus angularis (red bean) globulin. Food Chem 73:453-460 (2001).
33. Pallarès I, Vendrell J, Avilès FX and Ventura S, Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin.JMol Biol 342:321-331 (2004).
34. Dufour E, Hoa GH and Haertlé T, High-pressure effects of β-lactoglobulin interactions with ligands studied by fluorescence. BiochimBiophys Acta 1206:166-172 (1994).
35. Kelly SM, Jess TJ and Price NC, How to study proteins by circular dichroism. BiochimBiophys Acta 1751:119-139 (2005).
36. Kelly SM and Price NC, The application of circular dichroism to studies of protein folding and unfolding. Biochim Biophys Acta 1338:161-185 (1997).
37. Zirwer D, Gast K, Welfle H, Schlesier B and Schwenke KD, Secondary structure ofglobulins fromplant seeds:Are-evaluation from circular dichroism measurements. Int J BiolMacromol 7:105-108 (1985).
38. Li-Chan E, Nakai S and Wood DF, Hydrophobicity and solubility of meat protein and their relationship to emulsifying properties. J Food Sci 49:345-350 (1984).
39. Arntfield SD, Microstructural and rheological properties of protein networks from ovalbumin and vicilin. PhD thesis. University of Manitoba, Winnipeg (1989).