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Purification and characterization of a dipeptidase from Lactobacillus sake
M C Montel1, M P Seronie, R Talon
1Station de Recherches sur la Viande, Institut National de la Recherche Agronomique, Saint-Genès Champanelle, France.
Applied and Environmental Microbiology
|February 1, 1995
Abstract:
A dipeptidase was purified from cell extracts of Lactobacillus sake. This compound was a monomer having a molecular weight of 50,000 and a pI of 4.7 and exhibited broad specificity against all dipeptides except those with proline or glycine at the N terminus. The enzyme was inhibited by EDTA or 1,10-phenanthroline but could be reactivated with CoCl2 and MnCl2.