Functional and nutritional properties of peanut and cowpea proteins

Journal of Food, Agriculture and Environment

Volumn 10, Issue 3-4, 2012, Pages 19-25

  Guang, Cuie ^a,b   Phillips, Robert Dick ^b   Shang, Jiangang ^a  

^a JIANGNAN UNIVERSITY   (China)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

Cowpea; Functional property; Nutritional quality; Peanut; Protein

Indexed keywords

ALBUMIN; AMINO ACID; ARGININE; GLOBULIN; GLUTENIN; HEMAGGLUTININ; LEUCINE; NITROGEN DERIVATIVE; PROLAMIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; VEGETABLE PROTEIN;

ABSORPTION; BIOAVAILABILITY; COWPEA; DIGESTIVE FUNCTION; EMULSION; FOOD INDUSTRY; FOOD INTAKE; FOOD PROCESSING; FOOD STORAGE; HYDROPHOBICITY; MEAL; MOLECULAR SIZE; NUTRITIONAL VALUE; PEANUT; PH; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN INTAKE; REVIEW;

EID: 84869108004     PISSN: 14590255     EISSN: 14590263     Source Type: Journal    
DOI: None     Document Type: Review

References (91)

1. Ofuya, Z. M. and Akhidue, V. 2005. The role of pulses in human nutrition: A review. J. Appl. Sci. Environ. Manag. 9:99-104.
2. Wang, C., Tang, Y., Wang, X., Chen, D., Cui, F., Chi, Y., Zhang, J. and Yu, S. 2011. Evaluation of groundnut genotypes from China for quality traits. J. SAT Agric. Res. 9:1-5.
3. Özcan, M. M. 2010. Some nutritional characteristics of kernel and oil of peanut (Arachis hypogaea L.). J. Oleo Sci. 59:1-5.
4. Atasie, V. N., Akinhanmi, T. F. and Oijodu, C. C. 2009. Proximate analysis and physico-chemical properties of groundnut (Arachis hypogaea L.). Pak. J. Nutr. 8:194-197.
5. Asibu, J. Y., Akromah, R., Safo-Kantanka, O., Adu-Dapaah, H. K., Ohemeng-Dapaah, S. and Agyeman, A. 2008. Chemical composition of groundnut, Arachis hypogaea (L) landraces. Afr. J. Biotechnol. 7:2203-2208.
6. Grosso, N. R., Nepote, V. and Guzmán, C. A. 2000. Chemical composition of some wild peanut species (Arachis L.) seeds. J. Agric. Food Chem. 48:806-809.
7. Grosso, N. R. and Guzmán, C. A. 1995. Chemical composition of aboriginal peanut (Arachis hypogaea L.) seeds from Peru. J. Agric. Food Chem. 43:102-105.
8. Grosso, N. R. and Guzmán, C. A. 1995. Lipid, protein, and ash contents and fatty acid and sterol composition of peanut (Arachis hypogaea L.) seeds from Ecuador. Peanut Sci. 22:84-89.
9. Grosso, N. R., Zygadlo, A. L., Lamarque, A. L., Maestri, D. M. and Guzmán, C. A. 1997. Proximate, fatty acid and sterol composition of aboriginal peanut (Arachis hypogaea L.) seeds from Bolivia. J. Sci. Food Agric. 73:349-356.
10. Grosso, N. R., Lucini, E. I., López, A. G. and Guzmán, C. A. 1999. Chemical composition of aboriginal peanut (Arachis hypogaea L.) seeds from Uruguay. Grasa y Aceites 50:203-207.
11. Ng, E. C., Dunford, N. T. and Chenault, K. 2008. Chemical characteristics and violet profile of genetically modified peanut cultivars. J. Biosci. Bioeng. 106:350-356.
12. Jonnala, R. S., Dundord, N. T. and Chenault, K. 2005. Nutritional composition of genetically modified peanut varieties. J. Food Sci. 70:254-256.
13. 2 levels. J. Agric. Food Chem. 45:3863-3866.
14. Sarvamangala, C., Gowda, M. V. C. and Varshney, R. K. 2011. Identification of quantitative trait loci for protein content, oil content and oil quality for groundnut (Arachis hypogaea L.). Field Crops Res. 122:49-59.
15. Özcan, M. and Seven, S. 2003. Physical and chemical analysis and fatty acid composition of peanut, peanut oil and peanut butter from COM and NC-7 cultivars. Grasa y Aceites 54:12-18.
16. Dwivedi, S. L., Nigam, S. N., Nageswara Rao, R. C., Singh, U. and Rao, K. V. S. 1996. Effects of drought on oil, fatty acids and protein contents of groundnut (Arachis hypogaea L.) seeds. Field Crops Res. 48:125-133.
17. Chiou, R. Y., Ku, K. and Chen, W. 1997. Compositional characterization of peanut kernels after subjection to various germination times. J. Agric. Food Chem. 45:3060-3064.
18. Parmer, D. L., Kumar, A. L. R. and Bharodia, P. S. 2002. Genetics and interrelationship of oil and protein content in crosses involving confectionary genotypes of groundnut (Arachis hypogaea L.). J. Oilseeds Res. 19:32-34.
19. Carvalho, A. F. U., de Sousa, N. M., Farias, D. F., da Rocha-Bezerra, L. C. B., da Silva, R. M. P., Viana, M. P., Gouveia, S. T., Sampaio, S. S., de Sousa, M. B., de Lima, G. P. G., de Morais, S. M., Barros, C. C. and Filho, F. R. F. 2012. Nutrional ranking of 30 Brazilian genotypes of cowpea including determination of antioxidant capacity and vitamins. J. Food Compos. Anal. 26:81-88.
20. Tchiagam, J. B., Bell, J. M., Nassourou, A. M., Njintang, N. Y. and Youmbi, E. 2011. Genetic ananlysis of seed proteins in cowpea (Vigna unguiculata L. Walp.). Afr. J. Biotechnol. 10:3077-3086.
21. Vasconcelos, I. M., Maia, F. M. M., Farias, D. F., Campello, C. C., Carvalho, A. F. U., Moreira, R. A. and de Oliveira, J. T. A. 2010. Protein fractions, amino acid composition and antinutritional constituents of high-yielding cowpea cultivars. J. Food Compos. Anal. 23:54-60.
22. Onwuliri, V. A. and Obu, J. A. 2002. Lipids and other constituents of Vigna unguiculata and Phaseolus vulgaris grown in northern Nigeria. Food Chem. 78:1-7.
23. Giami, S. Y. 2005. Compositional and nutritional properties of selected newly developed lines of cowpea (Vigna unguiculata L. Walp). J. Food Compos. Anal. 18:665-673.
24. Dekhane, S. S., Khafi, H. R., Raj, A. D. and Parmar, R. M. 2011. Effect of biofertilizer and fertility levels on yield, protein content and nutrient uptake of cowpea [Vigna unguiculata (L.) WALP.]. Legume Res. 34:51-54.
25. Andersen, P. C., Hill, K., Gorbet, D. W. and Brodbeck, B. V. 1998. Fatty acid and amino acid profiles of selected peanut cultivars and breeding lines. J. Food Compos. Anal. 11:110-111.
26. Ingale, S. and Shrivastava, S. K. 2011. Nutritional study of new variety of groundnut (Arachis hypogaea L.) JL-24 seeds. Afr. J. Food Sci. 5:490-498.
27. Iqbal, A., Khalil, I. A., Ateeq, N. and Khan, M. S. 2006. Nutritional quality of important food legumes. Food Chem. 97:331-335.
28. Chan, C. W. and Phillips, R. D. 1994. Amino acid composition and subunit constitution of protein fractions from cowpea (Vigna unguiculata L. Walp) seeds. J. Agric. Food Chem. 42:1857-1860.
29. Leticia, O. C., Fabiola, P. P., Erik, P. L., Miguel, O. N., José, R. B. and George, G. 2007. Composition and bioactive factor content of cowpea (Vigna unguiculata L. Walp) raw meal and protein concentrate. J. Sci. Food Agric. 87:112-119.
30. Marconi, E., Ruggeri, S. and Carnovale, E. 1997. Chemical evaluation of wild underexploited Vigna spp. seeds. Food Chem. 59:203-212.
31. Moure, A., Sineiro, J., DoMínguez, H. and Parajó, J. C. 2006. Functionality of oilseed protein products: A review. Food Res. Int. 39:945-963.
32. Poms, R. E., Capelletti, C. and Anklam, E. 2004. Effect of roasting history and buffer composition on peanut protein extraction efficiency. Mol. Nutri. Food Res. 48:459-464.
33. Yu, J., Ahmedna, M. and Goktepe, I. 2007. Peanut protein concentration: Production and functional properties as affected by processing. Food Chem. 103:121-129.
34. Mwasaru, M. A., Muhammad, K., Bakar, J. and Che Man, Y. B. 1999. Effects of isolation technique and conditions on the extractability, physicochemical and functional properties of pigeonpea (Cajanus cajan) and cowpea (Vigna unguiculata) protein isolates. I. Physicochemical properties. Food Chem. 67:435-443.
35. Cherry, J. P. 1990. Peanut protein and product functionality. JAOCS 67:5473-5481.
36. Woodroof, J. G. 1983. Composition and nutritive value of peanuts. In Woodroof, J. G. (ed.). Peanuts: Production, Processing, Products. AVI Publishing Co. Inc., Westport, pp. 165-179.
37. Nugdallah, G. A. and El Tinay, A. H. 1997. Effect of cooking on cowpea protein fractions. Plant Food. Hum. Nutr. 51:277-282.
38. Patil, U. G., Chavan, J. K., Kadam, S. S. and Salunkhe, D. K. 1993. Effects of dry heat treatments to peanut kernels on the functional properties of the defatted meal. Plant Foods Hum. Nutr. 43:157-162.
39. Kain, J. R. and Chen, Z. 2008. Effects of processing methods on the physico-functional properties of peanut flour (Arachis hypogaea L.). Biotechnol. 7:168-174.
40. Park, H. K., Sohn, K. H. and Kim, H. J. 1990. A study of the foaming properties of peanut protein isolate. Korean J. Soc. Food Sci. 6:9-15.
41. Horax, R., Hettiarachchy, N. S., Chen, P. and Jalaluddin, M. 2004. Functional properties of protein isolate from cowpea (Vigna unguiculata L. Walp.). J. Food Sci. 69:119-121.
42. Ragab, D. M., Babiker, E. E. and Eltinay, A. H. 2004. Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration. Food Chem. 84:207-212.
43. Wu, H., Wang, Q., Ma, T. and Ren, J. 2009. Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Res. Int. 42:343-348.
44. Damame, S. V., Chavan, J. K. and Kadam, S. S. 1990. Effects of roasting and storage on proteins and oil in peanut kernels. Plant Foods Hum. Nutr. 40:143-148.
45. Chiou, R. Y. Y. and Tsai, T. T. 1989. Characterization of peanut proteins during roasting as affected by initial moisture content. J. Agric. Food. Chem. 37:1377-1381.
46. Basha, S. M. and Young, C. T. 1985. Changes in polypeptide composition of peanut seed during oil roasting. J. Agric. Food Chem. 33:350-354.
47. Kopper, R. A., Odum, N. J., Sen, M., Helm, R. M., Stanley, J. S. and Burks, A. W. 2005. Peanut protein allergens: the effect of roasting on solubility and allergenicity. Int. Arch. Allergy Immunol. 136:16-22.
48. Ahmed, E. M. and Schmidt, R. H. 1979. Functional properties of peanut and soy proteins as influenced by processing methods. Peanut Sci. 6:1-6.
49. Hu, X., Zhao, M., Sun, W., Zhao, G. and Ren, J. 2011. Effects of microfluidization treatment and transglutaminase cross-linking on physiochemical, functional, and conformational properties of peanut protein isolate. J. Agric. Food Chem. 59:8886-8894.
50. Jacks, T. J., Hensarling, T. P. and Muller, L. L. 1983. Increased oilseed protein solubility after peroxide exposure. JAOCS 60:852.
51. Abu, J. O., Müller, K., Duodu, K. G. and Minnaar, A. 2006. Gamma irradiation of cowpea (Vigna unguiculata L. Walp) flours and pastes: Effects on functional, thermal and molecular properties of isolated proteins. Food Chem. 95:138-147.
52. Abu, J. O., Müller, K., Duodu, K. G. and Minnaar, A. 2005. Functional properties of cowpea (Vigna unguiculata L. Walp) flours and pastes as affected by γ-irradiation. Food Chem. 93:103-111.
53. Mwangwela, A. M., Waniska, R. D. and Minnaar, A. 2007. Effect of micronisation temperature (130 and 170°C) on functional properties of cowpea flour. Food Chem. 104:650-657.
54. Kinsella, J. E. 1976. Functional properties of food proteins: A survey. Crit. Rev. Food Sci. Nutr. 8:219-280.
55. Hu, X., Ren, J., Zhao, M., Cui, C. and He, P. 2011. Emulsifying properties of the transglutaminase-treated crosslinked product between peanut protein and fish (Decapterus maruadsi) protein hydrolysates. J. Sci. Food Agric. 91:578-585.
56. Yasumatsu, K., Sawada, K., Moritaka, S., Misaki, M., Toda, J., Wada, T. and Ishii, K. 1972. Whipping and emulsifying properties of soybean products. Agric. Biol. Chem. 36:719.
57. Aluko, R. E. and Yada, R. Y. 1999. Effect of a microbial calcium independent transglutaminase on functional properties of a partially purified cowpea (Vigna unguiculata) globulin. J. Sci. Food Agric. 79:286-290.
58. Gilani, G. S., Cockell, K. A. and Sepehr, E. 2005. Effects of antinutritional factors on protein digestibility and amino acid availability in foods. J. AOAC Int. 88:967-987.
59. Department of Health, South Africa. 2007. Guidelines relating to the regulations governing the labeling and advertising of foodstuffs. Accessed in June 2012 from http://www.doh.gov.za/docs/factsheets/guidelines/foodstuff/labelling01.pdf.
60. Umoren, U. E., Tewe, O. O., Bokanga, M. and Jackai, L. E. N. 1997. Protein quality of raw and autoclaved cowpeas: Comparison between some insect resistant and susceptible varieties. Plant Foods Hum. Nutr. 50:301-315.
61. Papadopoulos, M. C. 1989. Effect of processing on high-protein feedstuffs: A review. Biol. Waste. 29:123-138.
62. Hoffman, J. R. and Falvo, M. J. 2004. Protein-which is best? J. Sport. Sci. Med. 3:118-130.
63. Mcosker, D. E. 1961. The limiting amino acid sequence in raw and roasted peanut protein. J. Nutr. 76:453-459.
64. Jenkins, M. Y. and Mitchell, G. V. 1989. Nutritional assessment of twelve protein foods/ingredients. Nutr. Res. 9:83-92.
65. Miller, J. and Young, C. T. 1977. Protein nutritional quality of florunner peanut meal as measured by rat bioassay. J. Agric. Food Chem. 25:653-657
66. El-Niely, H. F. 2007. Effect of radiation processing on antinutrients, in-vitro protein digestibility and protein efficiency ratio bioassay of legume seeds. Radiat. Phys. Chem. 76:1050-1057.
67. Okeiyi, E. C. and Futrell, M. F. 1983. Evaluation of protein quality of formulations of sorghum grain flour and legume seeds. Nutr. Rep. Int. 28:451-461.
68. th edn. Benjamin Cummings, San Francisco, LA.
69. Khalil, S. K., Ahmed, I., Igbal, P. and Mufti, S. 1983. Nutritional and organoleptic evaluation of wheat bread supplemented with peanut flour. Pak. J. Sci. Indust. Res. 26:87-89.
70. Oyeleke, O. A., Morton, I. D. and Bender, A. E. 1985. The use of cowpea (Vigna unguiculata) in improving a popular Nigerian weaning food. Brit. J. Nutr. 54:343-347.
71. Sarwar, G. 1997. The protein digestibility-corrected amino acid score method overestimates quality of proteins containing antinutritional factors and of poorly digestible protein supplemented with limiting amino acids in rats. J. Nutr. 127:758-764.
72. rd edn. U.S. Dairy Export Council, Arlington, Virginia, 42 p.
73. Mensa-Wilmot, Y., Phillips, R. D. and Hargrove, J. L. 2001. Protein quality evaluation of cowpea-based extrusion cooked cereal/legume weaning mixtures. Nutr. Res. 21:849-857.
74. Tuan, Y., Phillips, R. D. and Dove, C. R. 1999. Predicting integrated protein nutritional quality. Part 1: Amino acid availability corrected amino acid score and nitrogen balance data fitted to linear and non-linear models for test proteins. Nutr. Res. 19:1791-1805.
75. Wang N., Shi, Y., Sun, J. and Le, G. 2007. Evaluation of peanut flour fermented with lactic acid bacteria as a probiotic food. Food Sci. Tech. Int. 13:469-475.
76. Stephens, A. M., Dean, L. L., Davis, J. P., Osborne, J. A. and Sanders, T. H. 2010. Peanuts, peanut oil, and fat free peanut flour reduced cardiovascular disease risk factors and the development of atherosclerosisin Syrian golden hamsters. J. Food Sci. 75(4):H116-H122.
77. Chen, G., Zhao, L., Bao, S. and Cong, T. 2006. Effects of different proteins on the metabolism of Zn, Cu, Fe, and Mn in rats. Biol. Trace Elem. Res. 113:165-175.
78. Wapnir, R. A. 1998. Copper absorption and bioavailability. Am. J. Clin. Nutr. 67:1054-1060.
79. Lönnerdal, B., Jayawickrama, L. and Lien, E. L. 1999. Effect of reducing the phytate content and of partially hydrolyzing the protein in soy formula on zinc and copper absorption and status in infant rhesus monkeys and rats pups. Am. J. Clin. Nutr. 69:490-496.
80. Megías, C., Pedroche, J., Yust, M. M., Girón-Calle, J., Alaiz, M., Millán, F. and Vioque, J. 2008. Production of copper-chelating peptides after hydrolysis of sunflower proteins with pepsin and pancreatin. Food Sci. Technol. 41:1973-1977.
81. Swain, J. H., Tabatabai, L. B. and Reddy, M. B. 2002. Histidine content of low molecular-weight beef proteins influences iron bioavailability in Caco-2 cells. J. Nutr. 132:245-251.
82. Etcheverry, P., Hawthorne, K. M., Liang, L. K., Abrams, S. A. and Griffin, I. J. 2006. Effect of beef and soy proteins on the absorption of non-heme iron and inorganic zinc in children. J. Am. Coll. Nutr. 25:34-40.
83. Shahidi, F. and Zhong, Y. 2008. Bioactive peptides. J. AOAC Int. 91:914-931.
84. Jimsheena, V. K. and Gowda, L. R. 2011. Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from arachin by simulated gastric digestion. Food Chem. 125:56-569.
85. Chen, G., Zhao, L., Zhao, L., Cong, T. and Bao, S. 2007. In vitro study on antioxidant activities of peanut protein hydrolysate. J. Sci. Food Agric. 87:357-362.
86. Guang, C. and Phillips, R. D. 2012. Microplate kinetic assay of ACE activity and response surface methodology of hydrolysis factors of peanut and cowpea flours by Alcalase. J. Food Agric. Environ. 10(1):58-63.
87. Quist, E. E., Phillips, R. D. and Saalia, F. K. 2009. Angiotensin converting enzyme inhibitory activity of proteolytic digests of peanut (Arachis hypogaea L.) flour. Food Sci. Tech. 42:694-699.
88. Guang, C. and Phillips, R. D. 2009. Purification, activity and sequence of angiotensin I converting enzyme inhibitory peptide from Alcalase hydrolysate of peanut flour. J. Agric. Food Chem. 57:10102-10106.
89. Guang, C. and Phillips, R. D. 2012. Performance of four sets of amino acid descriptor scales for evaluating quantitative structure-activity relationships of angiotensin I converting enzyme inhibitory dipeptides. J. Food Agric. Environ. 10(2):227-232.
90. Jimsheena, V. K. and Gowda, L. R. 2010. Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship. Peptides 31:1165-1176.
91. FAO/WHO 1990. Protein Quality Evaluation. Report of joint FAO/WHO Expert Consultation, Bethesda, MD, 4-8 December 1989. FAO/WHO, Rome, Italy.