Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN.
In: World journal of microbiology & biotechnology, Jg. 10 (1994-05-01), Heft 3, S. 256-9
Online
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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.
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| Autor/in / Beteiligte Person: | Elegado, FB ; Fujio, Y |
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| Zeitschrift: | World journal of microbiology & biotechnology, Jg. 10 (1994-05-01), Heft 3, S. 256-9 |
| Veröffentlichung: | 2005- : Berlin : Springer ; <i>Original Publication</i>: Oxford, OX, UK : Published by Rapid Communications of Oxford Ltd in association with UNESCO and in collaboration with the International Union of Microbiological Societies, c1990-, 1994 |
| Medientyp: | academicJournal |
| ISSN: | 0959-3993 (print) |
| DOI: | 10.1007/BF00414857 |
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