Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN
In: World Journal of Microbiology and Biotechnology, Jg. 10 (1994-05-01), Heft 3, S. 256-259
Online
serialPeriodical
Zugriff:
An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa. Its K m value for pectic acid was 2 mg/ml. It was stable at pH 4.5 to 11 and up to 50°C, with optimum activity at pH 4.5 to 4.75 and 55 to 60°C. Some ionic compounds enhanced the enzyme activity, whereas tannic acid at 0.5 mm caused about 90% inhibition.
Titel: |
Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN
|
---|---|
Autor/in / Beteiligte Person: | Elegado, F. B. ; Fujio, Y. |
Link: | |
Zeitschrift: | World Journal of Microbiology and Biotechnology, Jg. 10 (1994-05-01), Heft 3, S. 256-259 |
Veröffentlichung: | 1994 |
Medientyp: | serialPeriodical |
ISSN: | 0959-3993 (print) ; 1573-0972 (print) |
DOI: | 10.1007/BF00414857 |
Sonstiges: |
|