Purification and characterization of a dipeptidase from Lactobacillus sake. |
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| Authors: | M C Montel, M P Seronie, R Talon, M H braud |
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| Affiliation: | M C Montel, M P Seronie, R Talon, and M Hébraud |
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| 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. |
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