SOME PROPERTIES OF BETA-1,3-GLUCAN HYDROLYZING ENZYMES FROM THE ROTIFER BRACHIONUS PLICATILIS
K. Hara, H. Pangkey, K. Osatomi, K. Yatsuda, A. Hagiwara, K.
Tachibana, T. Ishihara-1997
Hydrobiologia, 358: 89-94 (from Current Contents)
Abstract:
We examined some characteristics of hydrolytic enzymes, especially
beta-1,3-glucanase, to obtain the information of cell wall lytic
enzymes for rotifers. Crude enzyme (ammonium sulfate fraction) of
rotifers hydrolyzed starch, beta-1,3-glucan, glycol chitin and CM-
cellulose. Optimum pH for hydrolysis of starch and CM-cellulose was
6.5, and that for beta-1,3 glucan and glycol chitin was pH 6.0. Pectic
acid, xylan and agarose were not hydrolyzed at pH 3-10. Beta-1,3
glucanase was purified about 73-fold from crude enzyme by ion-
exchange chromatography and gel filtration. Optimum pH and
temperature of the enzyme were 6 and 60 degrees C, respectively. The
molecular weight of the enzyme was estimated about 260 kDa by gel
filtration. The enzyme was inhibited by HgCl2 and MnCl2.
(Nagasaki Univ., Fac. Fisheries, 1-14 Bunkyo Machi, Nagasaki 852,
Japan)
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