Abstract

Rapid growth of global population should be demanded more high-quality food and this might be alleviated by improving protein nutrition levels in usual foodstuff. The expense associated with food additives used for animal production have led to the study of intracellular production of high-quality protein (HQP) by transgenic crops and other organisms, as a means of obtaining efficient and less costly sources of essential amino acids. One important approach is to extract high essential amino acids from bacteria or others. We designed a HQP gene encoding about 100 amino acids which had more than 80 % essential amino acids. GOR/Gibrat and Swiss-Pdb Viewer analysis were used to predict the secondary structure of HQP-1 in pI value, hydrophilic and hydrophobic properties. Then the HQP gene was transferred into E. coli BL21 (DE3), and the protein was extracted and identified by SDS-PAGE.

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