The aim of the study was to improve the protein content of biscuit; a low protein but widely consumed snack by schoolaged children. The study was carried out at the Department of Crop Utilization; International Institute of Tropical Agriculture (IITA), Ibadan between March, 2012 and December, 2012. Composite flour was produced from African yam bean (a nutrient-dense but underutilized legume) flour (AYBF) and wheat flour (WF).The composite flour was prepared at various ratios WF/AYBF 100:0, 80:20, 70:30 and 60:40.and used to produce biscuits. These biscuits samples were analysed and the 100/0 WF: AYBF biscuit served as control. Proximate analysis, crispness (breaking force) and sensory evaluation of the biscuit samples were determined using standard methods. Proximate analysis showed significant increase (P=.05) in protein (9.61-14.71%), ash (1.37-2.42%) and sugar (14.11-21.29%) and significant decrease in starch (76.66-51.15%) and fat (12.53-8.13%) contents with increase in AYBF in the biscuits. There was no significant difference in the moisture contents of the test samples. Crispness of the biscuit increased with increase in percentage of AYBF in the flour blend. The breaking force values reduced from 8.5kg (for 100/0 WF: AYBF biscuits) to 3.0kg (60/40 WF: AYBF biscuits). Lower breaking force was found to correspond with higher crispness. Sensory evaluation results showed that all biscuit samples had high rating for all evaluated attributes. The closeness of values obtained for all biscuit samples to the control sample indicate a high level of acceptance of the AYBF-WF biscuits. Hence, suggesting a way of obtaining biscuits with higher protein content.

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This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications. Sesame seed protein fractions were prepared according to their solubility: water-soluble (albumin), salt-soluble (globulin), alkaline-soluble (glutelin) and ethanol-soluble (prolamin). Globulin was the most abundant fraction, consisting of 91% protein, followed by glutelin, albumin and prolamin in decreasing order. Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed polypeptides of sizes ≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19, 85 and 100 kDa. Prolamin had polypeptide sizes 20, 40 and 100 kDa. The albumin and globulin fractions had higher intrinsic fluorescence intensity (FI) values than the glutelin. Albumin had a higher solubility (ranging from 80 to 100%) over a wide pH range when compared with the other fractions. Water holding capacity (g/g) reduced from 2.76 (glutelin) to 1.35 (prolamin) followed by 0.42 (globulin) and 0.08 (albumin). Oil holding capacity (g/g) reduced from: 4.13 (glutelin) to 2.57 (globulin) and 1.56, 1.50 for albumin and prolamin respectively. Gelling ability was stronger for prolamin and glutelin than albumin and globulin, while higher emulsion (p < 0.05) quality was obtained for prolamin and albumin than for glutelin and globulin. Graphical abstract

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Conophor nut (Tetracarpidium conophorum) was processed using different heat treatments to explore its full potential as food ingredients. The raw, boiled, and toasted nuts were defatted and the proteins isolated by alkaline solubilization and isoelectric precipitation. The variously processed nuts were analyzed for the proximate and amino acid compositions, and functional properties. The protein contents of the isolate ranges between 86.86 g/100g and 87.74 g/100 g, about 1.5‐fold higher than those of the defatted flour samples. The essential amino acids of the isolates ranged between 40.57%–41.55%. Glutamic acid, aspartic acid, and arginine were the most predominant amino acids, while methionine and lysine were the first and second limiting amino acids, respectively. The protein efficiency ratio, biological values as well as the functional properties of the proteins were improved with processing. These properties may enhance the potential use of conophor nut protein isolates as high‐quality protein ingredient in food systems.