Cargando…
Characterization of the Recombinant Exopeptidases PepX and PepN from Lactobacillus helveticus ATCC 12046 Important for Food Protein Hydrolysis
The proline-specific X-prolyl dipeptidyl aminopeptidase (PepX; EC 3.4.14.11) and the general aminopeptidase N (PepN; EC 3.4.11.2) from Lactobacillus helveticus ATCC 12046 were produced recombinantly in E. coli BL21(DE3) via bioreactor cultivation. The maximum enzymatic activity obtained for PepX was...
Autores principales: | Stressler, Timo, Eisele, Thomas, Schlayer, Michael, Lutz-Wahl, Sabine, Fischer, Lutz |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3716637/ https://www.ncbi.nlm.nih.gov/pubmed/23894590 http://dx.doi.org/10.1371/journal.pone.0070055 |
Ejemplares similares
-
Draft Genome Sequence of Lactobacillus helveticus ATCC 12046
por: Palomino, María Mercedes, et al.
Publicado: (2018) -
PepX: a structural database of non-redundant protein–peptide complexes
por: Vanhee, Peter, et al.
Publicado: (2010) -
The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S
por: Yu, Guiyang, et al.
Publicado: (2015) -
Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481
por: Stressler, Timo, et al.
Publicado: (2012) -
Comparative analysis of homologous aminopeptidase PepN from pathogenic and non-pathogenic mycobacteria reveals divergent traits
por: Sharma, Nishant, et al.
Publicado: (2019)