Abstract
At least fourteen or fifteen kinds of endo-xylanase components (endo-X) were found to participate in the xylan-hydrolysing activity of the mid-gut gland of the apple snail (Pomacea canaliculata). One of these endo-X was purified to electrophoretic homogeneity from the mid-gut glands of the female snails. Its molecular weight and isoelectric point were estimated to be about 42,000 by SDS-PAGE and 7.45, respectively. The optimum pH of the enzyme reaction existed between 6.0–6.3, and the activity was stable from pH 4.5–9.0, and was stable for 15min at 40°C and pH 6.0. The activity of this enzyme rose markedly in the presence of some chlorides or sodium bromide, but not in the presence of sodium sulfate or sodium citrate.
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