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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| Vydáno v: | Appl Environ Microbiol |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
2000
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| Témata: | |
| On-line přístup: | 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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