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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הוצא לאור ב:	Appl Environ Microbiol
Principais autores:	Savijoki, Kirsi, Palva, Airi
פורמט:	Artigo
שפה:	Inglês
יצא לאור:	American Society for Microbiology (ASM) 2000
נושאים:	Enzymology and Protein Engineering
גישה מקוונת:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC91898/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10653753/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.66.2.794-800.2000
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