Efficient Method for the Purification of Recombinant Amaranth 11S Globulins with Angiotensin-Converting Enzyme Inhibitory Activity

Amaranth 11S globulin is a plant protein that is renowned for its high essential amino acid content and nutritional value. It has undergone modification through the insertion of antihypertensive peptides valine-tyrosine (VY), which act as angiotensin-converting enzyme (ACE) inhibitors. The expression of this protein was carried out in E. coli. Despite the potential of this protein, an efficient purification method is still required to allow its evaluation and subsequent application. This work proposes a procedure that allows for high purification and yield. After obtaining the purified proteins from the inclusion bodies and purifying them in an insoluble form, it was determined that this process did not affect their bioactivity.