Stability of native and modified α-galactosidase of Cladosporium cladosporioides
| Autor: | N. V. Borzova, L. D. Varbanets |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: | |
| Zdroj: | The Ukrainian Biochemical Journal, Vol 87, Iss 4, Pp 5-12 (2015) |
| Druh dokumentu: | article |
| ISSN: | 2409-4943 2413-5003 |
| DOI: | 10.15407/ubj87.04.005 |
| Popis: | By modifying carbohydrate component of glycoproteins it is possible to elucidate its role in manifestation of structural and functional properties of the enzyme. The comparison of activity and stability of the native and modified by oxidation with sodium periodate α-galactosidase of Cladosporium cladosporioides was carried out. To determine α-galactosidase activity the authors used n-nitrophenyl synthetic substrate, as well as melibiose, raffinose and stachyose. Modification of the carbohydrate component had a significant effect on catalytic properties of the enzyme. Both the reduction of Vmax and enzyme affinity for natural and synthetic substrates were observed. The native enzyme retained more than 50% of the maximum activity in the range of 20-60 °C, while for the modified enzyme under the same conditions that temperature range was 30-50 °C. The modified α-galactosidase demonstrated a higher thermal stability under neutral pH conditions. The residual activity of the modified α-galactosidase was about 30% when treated with 70% (v/v) methanol, ethanol and propanol. About 50% of initial activity was observed when 40% ethanol and propanol, and 50% methanol were used. It was shown that the modification of C. cladosporioides α-galactosidase by sodium periodate is accompanied by a significant decrease in enzyme activity and stability, probably caused by topological changes in the tertiary and quaternary structure of the protein molecule. |
| Databáze: | Directory of Open Access Journals |
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