Purification and characterization of X-prolyl dipeptidyl peptidase fromLactobacillus casei subsp.casei LLG
In: Applied Microbiology and Biotechnology, Jg. 42 (1994-12-01), Heft 2-3, S. 280-286
Online
serialPeriodical
Zugriff:
X-Prolyl dipeptidyl peptidase, which hydrolysed X-Pro-Y almost specifically, has been purified to homogeneity from crude cell-free extracts ofLactobacillus casei subsp.casei LLG using fast protein liquid chromatography equipped with preparative and analytical anion exchange columns. The enzyme was purified to 274-fold by ammonium sulphate fractionation, and by two successive ion-exchange chromatographies with a recovery of 34%. The purified enzyme appeared as a single band on both native-polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulphate (SDS)-PAGE and had a molecular mass of 79 kDa. The pH and the temperature optima by the purified enzyme were 7.0 and 50°C, respectively. X-PDP was a serine-dependent enzyme, as both diisopropylfluorophosphate and phenylmethylsulphonylfluoride caused complete inhibition of the enzyme activity. The Michaelis constant (K m ) and maximum reaction velocity (V max ) values were 0.2 mm and 43 mm per milligram, respectively.
Titel: |
Purification and characterization of X-prolyl dipeptidyl peptidase fromLactobacillus casei subsp.casei LLG
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Autor/in / Beteiligte Person: | Habibi-Najafi, M. B. ; Lee, B. H. |
Link: | |
Zeitschrift: | Applied Microbiology and Biotechnology, Jg. 42 (1994-12-01), Heft 2-3, S. 280-286 |
Veröffentlichung: | 1994 |
Medientyp: | serialPeriodical |
ISSN: | 0175-7598 (print) ; 1432-0614 (print) |
DOI: | 10.1007/BF00902729 |
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