Glutaminase of Actinomucor taiwanensiswas purified approximately 96‐fold with a yield of 18%, by sequential fractionation with ammonium sul‐phate, anion exchange with DEAE‐Sepharose CL‐6B and gel filtration with Sephacryl S‐200. The pH and temperature optima of purified glutaminase were 8·0 and 45°C, respectively. Glutaminase was stable at a temperature up to 35°C and at pH values of 6·0–8·0. The molecular weight was 80000 as determined from SDS‐PAGE. The enzyme activity was markedly inhibited by HgCl2. In the presence of 100 g litre−1 NaCl, the enzyme activity was inhibited 50%.
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