Improvement of an unusual twin-arginine transporter leader peptide by a codon-based randomization approach
Por:
Monroy-Lagos O., Soberon X., Gaytan P., Osuna J.
Publicada:
1 ene 2006
Resumen:
Secretion of Escherichia coli penicillin acylase was improved by codon-based random mutagenesis of its signal peptide. The mutagenesis technology was applied to the gene region coding for positions Lys2 to Thrl3 (N half) and Ala14 to Leu25 (C half) of the signal peptide. Protein secretion was higher in several signal peptide variants (up to fourfold with respect to the wild-type value). Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Filiaciones:
Monroy-Lagos O.:
Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad National Autónoma de México, Cuernavaca, Mexico
Soberon X.:
Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad National Autónoma de México, Cuernavaca, Mexico
Gaytan P.:
Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad National Autónoma de México, Cuernavaca, Mexico
Osuna J.:
Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad National Autónoma de México, Cuernavaca, Mexico
Instituto de Biotecnologia, UNAM, Av. Universidad 2001, 62210 Cuernavaca, Morelos, Mexico
All Open Access, Bronze
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