| Autor: |
Marco Gobbetti, Aldo Corsetti, Patrick F. Fox, E. Smacchi, L. Stepaniak |
| Jazyk: |
angličtina |
| Rok vydání: |
1996 |
| Předmět: |
|
| Zdroj: |
Scopus-Elsevier |
| Popis: |
Peptide hydrolase and proteinase activities of nine strains (eight species) of sourdough homo- and heterofermentative Lactobacillus were determined and their subcellular distribution localized. Aminopeptidase, dipeptidase, tripeptidase and iminopeptidase activities were measurable in all strains, but all four activities were highest in L. brevis subsp. lindneri CBI and A79. Low carboxypeptidase activity was detected in L. fructivorans DD1 and L. plantarum DC400 only. While aminopeptidase and iminopeptidase activity was detected mainly in the cytoplasmic fraction, dipeptidase and tripeptidase activity was found to be associated with the cell wall and membrane. Activity of endopeptidase on methionine enkephalin was quite similar in all strains and more than 90% of this activity was located in the cytoplasm. The level of proteolytic activity on casein and gluten was very variable and strain-dependent. Proteolytic activity was detected only in the cytoplasm and cell wall-associated fractions. Heterofermentative L. brevis subsp. lindneri strains and homofermentative L. plantarum DC400 and L. farciminis CC1 accumulated the highest level of free amino acids at the end of sourdough fermentation. These strains showed high proteolytic acitivity on gluten and especially high peptidase activities. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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