Consulta: subjectFacets:"Protein engineering"
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Data/hora: 27/07/2024 03:07:29

Expression, purification and thermal stability evaluation of an engineered amaranth protein expressed in Escherichia coli
Provedor de dados: Electronic Journal of Biotechnology
Autores: Morales-Camacho,Jocksan I; Paredes-López,Octavio; Espinosa-Hernández,Edgar; Fernández Velasco,Daniel Alejandro; Luna-Suárez,Silvia.
Background: The acidic subunit of amarantin (AAC)-the predominant amaranth seed storage protein-has functional potential and its third variable region (VR) has been modified with antihypertensive peptides to improve this potential. Here, we modified the C-terminal in the fourth VR of AAC by inserting four VY antihypertensive peptides. This modified protein (AACM.4) was expressed in Escherichia coli. In addition, we also recombinantly expressed other derivatives of the amarantin protein. These include: unmodified amarantin acidic subunit (AAC); amarantin acidic subunit modified at the third VR with four VY peptides (AACM.3); and amarantin acidic subunit doubly modified, in the third VR with four VY peptides and in the fourth VR with the RIPP peptide...
Tipo: Journal article
Palavras-chave: Globulin 11S; Protein expression; Protein engineering; Thermal stability.
Ano: 2016
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000400007