Journal of Biotechnology & Biomaterials
Open Access

Abstract

Food proteins play different roles, one of them is to provide nutrients to maintain the body, besides, they may exert nutraceutical effects like providing health benefits that can be used for treatment or prevention of diseases. In this sense, the storage proteins of plants can be modified in its primary structure to confer any specific feature; the modifications have to change to the minimum the original features of the protein. In this work were modified two variable regions of the acidic peptide of the 11S amaranth globulin (amarantin). The mutant proteins were expressed in E. coli Origami (DE3). The expression of the amarantin acidic polipeptide in the fourth variable region (ACR4) suggest that it is as stable as the complete amarantin (Medina-Godoy et al., 2004) and as the unmodified amarantin acidic polypeptide (Luna-Suárez et al., 2008) and it appear more stable than amarantin acidic subunit modified in the third variable region (ACR3). According to the densitometry analysis; the maximum level of protein expression observed after induction for 3 h was estimated to be 6.5mg of ACR3 per liter of culture; and 34 mg of ACR4 /L at 6h. The accumulation of ACR4 was maintained up 20 h and 6h for ACR3. The tests confirmed that the insertion of the antihypertensive peptide subunit VY in the fourth variable region of amarantin acidic subunit did not dramatically affect the expression of this protein like the third variable region modified did.

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