| Autor: |
Azhari, Rosa, Szlak, Alda M., Ilan, Ehud, Sideman, Samuel, Lotan, Noah |
| Zdroj: |
Biotechnology & Applied Biochemistry; 1989, Vol. 11 Issue 1, p105-117, 13p |
| Abstrakt: |
A crude inulinase preparation, from Aspergillus, was fractioned in a sequence of operations, including ion exchange chromatography on CM-Sepharose and high-performance gel permeation chromatography. Two highly purified inulin-degrading enzymes were thus obtained and some of their characteristics were established. The first enzyme had an endo-type activity, a Mr of 53,000, and Km = 570 mm (in terms of glycosidic bonds). The second was of the exo-type, and has a Mr of 81,000 and Km = 60 mm (in terms of inulin chains). The two enzymes are highly activated (up to 20-fold) by Fe3+ and partially inhibited by Mn2+ and Mg2+. Both enzymes also exhibit invertase activity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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