[1]
Onimawo IA, Oteno F, Orokpo G, Okubor PI. Physicochemical and nutrient evaluation of African bush mango (Irvingia gabonensis) seeds and pulp. Plant Foods Hum Nutr 2003; 58: 1-6.
[2]
Joseph JK. Physico-chemical attributes of wild mango (Irvingia gabonensis) seeds. Bioresour Technol 1995; 53(2): 179-81.
[3]
Ejiofor MAN, Onwubuke SN, Okafor JC. Developing improved methods of processing and utilization of kernels of Irvingia gabonensis (var. gabonensis and var. excelsa). Int Tree Crops J 1987; 4(4): 283-90.
[4]
Oboh G, Ekperigin MM. Nutritional evaluation of some Nigerian wild seeds. Mol Nutr Food Res 2004; 48(2): 85-7.
[5]
Giami SY, Okonkwo VI, Akusu MO. Chemical composition and functional properties of raw, heat-treated and partially proteolysed wild mango (Irvingia gabonensis) seed flour. Food Chem 1994; 49(3): 237-43.
[6]
Ndjouenkeu R, Akingbala JO, Oguntimein GB. Emulsifying properties of three African food hydrocolloids: okra (Hibiscus esculentus), dika nut (Irvingia gabonensis), and khan (Belschmiedia sp.). Plant Foods Hum Nutr 1997; 51(3): 245-55.
[7]
Adamson I, Okafor C, Abu-Bakare A. A supplement of Dikanut (Irvingia gabonesis) improves treatment of type II diabetics. West Afr J Med 1989; 9(2): 108-15.
[8]
Ngondi JL, Oben JE, Minka SR. The effect of Irvingia gabonensis seeds on body weight and blood lipids of obese subjects in Cameroon. Lipids Health Dis 2005; 4(1): 12.
[9]
Kinsella JE, Melachouris N. Functional properties of proteins in foods: A survey. Crit Rev Food Sci Nutr 1976; 7(3): 219-80.
[10]
Cano-Medina A, Islas HJ, Dendooven L, Herrera RP, Alatorre GG. Escamilla-Silva. Emulsifying and foaming capacity and emulsion and foam stability of sesame protein concentrates. Food Res Int 2011; 44: 684-92.
[11]
Mune Mune MA, Sogi DS. Emulsifying and foaming properties of protein concentrates prepared from cowpea and bambara bean using different drying methods. Int J Food Prop 2016; 19: 371-84.
[12]
Zayas JF. Functionality of proteins in foods Springer: New York 1997.
[13]
Lu Q, Zhang Y, Wang Y, et al. California Hass avocado: Profiling of carotenoids, tocopherols, fatty acids and fat content during maturation and from different growing areas. J Agric Food Chem 2009; 57(21): 10408-13.
[14]
AOAC. Official methods of analysis. 15th ed. Arlington: Association of Official Analytical Chemists 1990.
[15]
Hellwig M, Matthes R, Peto A, Löbner J, Henle T. N-epsilon-fructosyllysine and N-epsilon-carboxyme-thyllysine but not lysinoalanine are available for absorption after simulated gastrointestinal digestion. Amino Acids 2014; 46: 289-99.
[16]
Hellwig M, Henle T. Release of pyrraline in absorbable peptides during simulated digestion of casein glycated by 2-deoxyglucose. Eur Food Res Technol 2013; 237: 47-55.
[17]
Hurrell RF, Lerman P, Carpenter KJ. Reactive lysine in foodstuffs as measured by a rapid dye - binding pro cedure. J Food Sci 1979; 44: 1221-7.
[18]
Mune Mune MA, Nyobe EC, Bassogog CB, Minka SR. A comparison on the nutritional quality of proteins from Moringa oleifera leaves and seeds. Cogent Food Agric 2016; 2(1): 1213618.
[19]
FAO/WHO. Protein quality evaluation. Food and Agricultural Organization of the United Nations Rome, Italy 1991.
[20]
Alsmeyer RH, Cunningham AE, Happich ML. Equations predict PER from amino acid analysis. Food Technol 1974; 28: 34-40.
[21]
Oser BL. An integrated essential amino acid index for predicting
the biological value of proteins In: Albanese AA, Ed Protein and
amino acid nutrition Academic Press: New York 1959; pp. 295-
311.
[22]
Mørup IK, Olesen ES. New method for prediction of protein value from essential amino acid pattern. Nutr Rep Int 1976; 13: 355-65.
[23]
Chelh I, Gatellier P, Sante-Lhoutellier V. A simplifier procedure for Myofibril hydrophobicity determination. Meat Sci 2006; 74(4): 681-3.
[24]
Mune Mune MA, Bakwo Bassogog CB, Nyobe EC, Minka SR. Physicochemical and functional properties of Moringa oleifera seed and leaf flour. Cogent Food Agric 2016; 2(1): 1220352.
[25]
Farrell HM Jr, Wickham ED, Unruh JJ, Qi PX, Hoagland PD. Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocoll 2001; 15: 341-54.
[26]
Lawal O. Functionality of African locust bean (Parkia biglobossa) protein isolate: Effect of pH, ionic strength and various protein concentrations. Food Chem 2004; 86: 345-55.
[27]
Myers RH, Montgomery DC. Response surface methodology:
Process and product optimization using designed experiments 2nd
ed Wiley: New York 2002.
[28]
Rebello CJ, Greenway FL, Finley JW. A review of the nutritional value of legumes and their effects on obesity and its related co‐morbidities. Obes Rev 2014; 15(5): 392-407.
[29]
Pastor‐Cavada E, Juan R, Pastor JE, Alaiz M, Vioque J. Nutritional characteristics of seed proteins in 28 Vicia species (Fabaceae) from Southern Spain. J Food Sci 2011; 76(8): C1118-24.
[30]
Rangel A, Saraiva K, Schwengber P, et al. Biological evaluation of a protein isolate from cowpea (Vigna unguiculata) seeds. Food Chem 2004; 87(4): 491-9.
[31]
Mubarak AE. Nutritional composition and antinutritional factors of mung bean seeds (Phaseolus aureus) as affected by some home traditional processes. Food Chem 2005; 89(4): 489-95.
[32]
Waller G, Feather M. The maillard reactions in foods and nutrition
American Chemical Society: Washington DC 1983.
[33]
Deosthale YG, Mohan VS, Rao KV. Varietal deficiencies in protein lysine and leucine content of gram sorghum. J Agric Food Chem 1970; 18: 644-6.
[34]
Achouri A, Nail V, Boye JI. Sesame protein isolate: Fractionation, secondary structure and functional properties. Food Res Int 2012; 46: 360-9.
[35]
Mune Mune MA, Sogi DS, Minka SR. Response surface methodology for investigating structure-function relationship of grain legume proteins. J Food Process Preserv 2017; 42(5): e13524.
27
3