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Journal of Undergraduate Research

Keywords

ã-zeins, lysine inserts, stable protein bodies, transgenic tobacco endosperm

College

Life Sciences

Department

Plant and Wildlife Sciences

Abstract

Maize is one of the most abundantly produced grains on earth and is widely used in human and livestock diets. 90% of maize protein is found in the endosperm portion of the seed in the form of small spherical aggregates called protein bodies. These protein bodies consist of four structurally distinct alcohol soluble proteins called á-, â-, ã-, and ä-zeins.1 Initial stages of protein body formation involve â- and ãzeins forming spherical accretions which later enlarge by the accumulation of á-zeins inside the â- and ãzein spheres.2 á-Zeins alone constitute 70% of the protein body and therefore make up a very substantial fraction of maize storage proteins. á-Zeins are also completely void of lysine, an essential amino acid. Maize alone, therefore, lacks adequate levels of lysine to maintain good nutrition. Societies that depend on corn as the main staple of their diet often deprive themselves of sufficient lysine and can become malnourished. If á-zein genes could be modified to include lysine, without disrupting protein body formation and other endosperm properties, the nutritional value of maize would be significantly enhanced.

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