Purification, Characterization, Gene Cloning, Sequencing, and Overexpression of Aminopeptidase N from Streptococcus thermophilus A

The general aminopeptidase PepN from Streptococcus thermophilus A was purified to protein homogeneity by hydroxyapatite, anion-exchange, and gel filtration chromatographies. The PepN enzyme was estimated to be a monomer of 95 kDa, with maximal activity on N-Lys–7-amino-4-methylcoumarin at pH 7 and 3...

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Detalhes bibliográficos

Publicado no:	Appl Environ Microbiol
Principais autores:	Chavagnat, Frederic, Casey, Michael G., Meyer, Jacques
Formato:	Artigo
Idioma:	Inglês
Publicado em:	American Society for Microbiology (ASM) 1999
Assuntos:	Food Microbiology
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC91448/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10388695/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.65.7.3001-3007.1999
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