The importance of dietary protein in human health: combating protein deficiency in sub-Saharan Africa through transgenic biofortified sorghum.

Child malnutrition is increasing in Africa. Protein deficiency is an important cause since protein is essential for both growth and maintenance of muscle mass. Sorghum is a major staple food in Africa on account of its hardiness as a crop. However, sorghum protein is very deficient in the indispensable amino acid lysine and on cooking has poor protein digestibility. This results in sorghum having a very low Protein Digestibility Corrected Amino Acid Score (PDCAAS). The Africa Biofortified Sorghum project, a Grand Challenges in Global Heath project, is undertaking research to biofortify sorghum in terms of protein and micronutrient quality using genetic engineering. Lysine and protein digestibility have been improved by suppression of synthesis of the kafirin storage proteins. Transgenic biofortified sorghum has double the PDCAAS of conventional sorghum. This improvement should enable a young child to meet most of its protein and energy requirements from biofortified sorghum porridge. This together with the improvement in micronutrients could provide the basis of a sustainable and broadly comprehensive solution to child malnutrition in many African countries.

Alteration of kafirin and kafirin film structure by heating with microwave energy and tannin complexation.

Heating with microwave energy and tannin complexation of kafirin both increase the tensile strength of cast kafirin bioplastic films. The effects of these treatments on the molecular structure of kafirin and of kafirin in the film were investigated. SDS-PAGE of heated wet kafirin showed an increase in kafirin oligomers. Disulfide groups increased in heated kafirin and in films made from the heated kafirin. Fourier transform infrared (FTIR) spectroscopy of heated kafirin and films made from the heated kafirin indicated an increase in beta-sheet conformation. In contrast, kafirin complexation with tannic acid (TA) and sorghum condensed tannin (SCT) resulted in a slight decrease in beta-sheet conformation in the kafirin and a larger decrease in the kafirin in the films. Raman spectroscopy showed that, with TA, there was a shift in peak from 1710 to 1728 cm(-1) for kafirin-tannic acid complexes, indicating kafirin and tannic acid interaction. The protein conformational changes presumably facilitated cross-linking between kafirin molecules and/or between kafirin and the tannins. Thus, although both heating with microwave energy and tannin complexation cause cross-linking of kafirin to increase film tensile strength, their effects on kafirin structure appear to be different.