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Purification and Molecular Characterization of a Tripeptidase (PepT) from Lactobacillus helveticus

A tripeptidase (PepT) from a thermophilic dairy starter strain of Lactobacillus helveticus was purified by four chromatographic steps. PepT appeared to be a trimeric metallopeptidase with a molecular mass of 150 kDa. PepT exhibited maximum activity against hydrophobic tripeptides, with the highest a...

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Detalles Bibliográficos
Main Authors: Savijoki, Kirsi, Palva, Airi
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Microbiology 2000
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC91898/
https://ncbi.nlm.nih.gov/pubmed/10653753
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