| Автор | Soda, Morsi El |
| Автор | Desmazeaud, Michel J. |
| Автор | Bergère, J.-L. |
| Дата выпуска | 1978 |
| dc.description | SummaryDiscovery of an endopeptidase by gel chromatography and separation of 3 exopeptidases (a dipeptidase, an aminopeptidase and a specific carboxypeptidase) from Lactobacillus casei NCDO 151 by affinity chromatography is described. The 3 exopeptidases were strongly inhibited by the metal chelators EDTA and 1,10-phenanthroline but were reactivated with Co<sup>2+</sup> and Mn<sup>2+</sup>. The pH optima for aminopeptidase, dipeptidase and carboxypeptidase activities were 6·5, 7·6 and 7·2, respectively. Maximum activity was obtained at 45 °C for the aminopeptidase, at 30 °C for the dipeptidase and at 40 °C for the carboxypeptidase.The substrate specificities of the 3 enzymes were also studied. The properties of these 3 enzymes are compared with those of other bacteria. |
| Формат | application.pdf |
| Издатель | Cambridge University Press |
| Копирайт | Copyright © Proprietors of Journal of Dairy Research 1978 |
| Название | Peptide hydrolases of Lactobacillus casei: isolation and general properties of various peptidase activities |
| Тип | research-article |
| DOI | 10.1017/S0022029900016666 |
| Electronic ISSN | 1469-7629 |
| Print ISSN | 0022-0299 |
| Журнал | Journal of Dairy Research |
| Том | 45 |
| Первая страница | 445 |
| Последняя страница | 455 |
| Аффилиация | Soda Morsi El; Institut National de la Recherche Agronomique |
| Аффилиация | Desmazeaud Michel J.; Institut National de la Recherche Agronomique |
| Аффилиация | Bergère J.-L.; Institut National de la Recherche Agronomique |
| Выпуск | 3 |
