The isoenzyme composition of b-1,3-glucanase of wheat seedlings was studied. According to the data of native isoelectric focusing, in the stem and root of 7-day-old seedlings the enzyme is represented by 7—8 isoforms with a wide pI range from 3.5 to 9.0. In germinating seed the spectrum is less heterogeneous and consisted only of acidic and alcaline forms (up to 5 components). Differences in the localization of b-1,3-glucanases were revealed: alcaline and neutral isoenzymes are located inside the cells, and acidic isoenzymes mainly in the intercellular space. Isoforms of the enzyme had different resistance to elevated temperature. Alcaline components are more thermostable and withstand heating for 10 min at 60 °C, while acidic and neutral have been inactivated at this temperature. Heating at 70 °C completely inhibited the enzyme activity. The activity of b-1,3-glucanase depends on the presence of metal cations. Copper cations had a pronounced inhibitory effect, while other studied cations — Ca2+, Ва2+ and to a lesser extent Mg2+ — increased the enzyme activity.
Keywords: i>Triticum aestivum L., seedlings, b-1,3-glucanase, isoenzymes
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